P49419 (AL7A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-aminoadipic semialdehyde dehydrogenase
Short name=Alpha-AASA dehydrogenase
EC=1.2.1.31

Alternative name(s):
Aldehyde dehydrogenase family 7 member A1
EC=1.2.1.3
Antiquitin-1
Betaine aldehyde dehydrogenase
EC=1.2.1.8
Delta1-piperideine-6-carboxylate dehydrogenase
Short name=P6c dehydrogenase

Gene names

Name:	ALDH7A1
Synonyms:	ATQ1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	539 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism. Ref.7 Ref.8
Catalytic activity	(S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H. Betaine aldehyde + NAD+ + H2O = betaine + NADH. An aldehyde + NAD+ + H2O = a carboxylate + NADH.
Pathway	Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1.
Subunit structure	Homotetramer By similarity.
Subcellular location	Mitochondrion. Nucleus Ref.7. Isoform 2: Cytoplasm › cytosol Ref.7.
Tissue specificity	Abundant in hepatoma cells and fetal cochlea, ovary, eye, heart, adrenal gland, liver and kidney. Low levels present in adult peripheral blood leukocytes and fetal brain, thymus, spleen, skeletal muscle, lung and tongue. Ref.1 Ref.5
Involvement in disease	Pyridoxine-dependent epilepsy (PDE) [MIM:266100]: Characterized by a combination of various seizure types. It usually occurs in the first hours of life and is unresponsive to standard anticonvulsants, responding only to immediate administration of pyridoxine hydrochloride. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9
Sequence similarities	Belongs to the aldehyde dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: KM=28.5 µM for nonanal Ref.7 KM=5.3 µM for trans-2-nonenal KM=39.1 µM for hexanal KM=17.5 µM for octanal KM=41.1 µM for betaine aldehyde KM=169 µM for L-2-aminoadipate 6-semialdehyde KM=530.2 µM for benzaldehyde KM=647.4 µM for propanal KM=7374.3 µM for glyceraldehyde Vmax=364.9 nmol/min/mg enzyme toward nonanal Vmax=34.9 nmol/min/mg enzyme toward trans-2-nonenal Vmax=243.3 nmol/min/mg enzyme toward hexanal Vmax=72.3 nmol/min/mg enzyme toward octanal Vmax=101.4 nmol/min/mg enzyme toward betaine aldehyde Vmax=276.2 nmol/min/mg enzyme toward L-2-aminoadipate 6-semialdehyde Vmax=125.2 nmol/min/mg enzyme toward benzaldehyde Vmax=69.9 nmol/min/mg enzyme toward propanal Vmax=174 nmol/min/mg enzyme toward glyceraldehyde
Sequence caution	The sequence AAC51935.1 differs from that shown. Reason: Frameshift at positions 233 and 268. The sequence AAH02515.3 differs from that shown. Reason: Erroneous initiation. The sequence AAH71712.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH73174.1 differs from that shown. Reason: Erroneous initiation. The sequence BAG35366.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Epilepsy
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular aldehyde metabolic process Inferred from sequence or structural similarity. Source: UniProtKB cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome glycine betaine biosynthetic process from choline Inferred from electronic annotation. Source: UniProtKB-UniPathway lysine catabolic process Traceable author statement. Source: Reactome sensory perception of sound Traceable author statement Ref.5. Source: ProtInc
Cellular_component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial matrix Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	L-aminoadipate-semialdehyde dehydrogenase activity Inferred from experiment. Source: Reactome aldehyde dehydrogenase (NAD) activity Inferred from sequence or structural similarity. Source: UniProtKB betaine-aldehyde dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EPS8	Q12929	2	EBI-726842,EBI-375576

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P49419-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P49419-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Isoform 3 (identifier: P49419-3)

The sequence of this isoform differs from the canonical sequence as follows:
     31-222: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: P49419-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGSPGRGAGLYFSSSQGLGLIPSPGLSM
     337-400: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 26

26

Mitochondrion Potential

Chain

27 – 539

513

Alpha-aminoadipic semialdehyde dehydrogenase

PRO_0000056490

Regions

Nucleotide binding

274 – 279

6

NAD By similarity

Sites

Active site

296

1

Proton acceptor By similarity

Active site

330

1

Nucleophile

Site

195

1

Transition state stabilizer By similarity

Natural variations

Alternative sequence

1 – 28

28

Missing in isoform 2.

VSP_038987

Alternative sequence

1

1

M → MGSPGRGAGLYFSSSQGLGL IPSPGLSM in isoform 4.

VSP_045904

Alternative sequence

31 – 222

192

Missing in isoform 3.

VSP_038988

Alternative sequence

337 – 400

64

Missing in isoform 4.

VSP_045905

Natural variant

199

1

A → V in PDE. Ref.8

VAR_031718

Natural variant

202

1

G → V in PDE. Ref.9

VAR_069184

Natural variant

291

1

G → E in PDE. Ref.9

VAR_069185

Natural variant

301

1

N → I in PDE. Ref.9

VAR_069186

Natural variant

335

1

R → Q in PDE. Ref.9

VAR_069187

Natural variant

395

1

V → G in PDE. Ref.9

VAR_069188

Natural variant

412

1

T → A.
Corresponds to variant rs2306618 [ dbSNP | Ensembl ].

VAR_028202

Natural variant

427

1

E → Q in PDE. Ref.8 Ref.9

VAR_031719

Natural variant

439

1

K → Q. Ref.4
Corresponds to variant rs12514417 [ dbSNP | Ensembl ].

VAR_028203

Natural variant

458

1

S → N in PDE. Ref.9

VAR_069189

Experimental info

Sequence conflict

236

1

K → R in BAG59812. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

539

Helix Strand Turn

Details...

Helix

33 – 35

3

Helix

37 – 45

9

Beta strand

49 – 52

4

Beta strand

54 – 60

7

Beta strand

65 – 69

5

Turn

71 – 73

3

Beta strand

76 – 81

6

Helix

85 – 102

18

Helix

107 – 123

17

Helix

125 – 135

11

Helix

140 – 160

21

Turn

161 – 163

3

Beta strand

167 – 169

3

Beta strand

176 – 184

9

Beta strand

186 – 191

6

Beta strand

194 – 196

3

Helix

199 – 210

12

Beta strand

214 – 218

5

Helix

221 – 223

3

Helix

224 – 240

17

Helix

245 – 247

3

Beta strand

248 – 251

4

Helix

255 – 263

9

Beta strand

268 – 274

7

Helix

276 – 288

13

Beta strand

292 – 296

5

Beta strand

301 – 305

5

Helix

311 – 323

13

Helix

324 – 327

4

Beta strand

333 – 339

7

Turn

340 – 342

3

Helix

343 – 355

13

Helix

375 – 390

16

Beta strand

394 – 397

4

Beta strand

403 – 407

5

Beta strand

412 – 416

5

Helix

422 – 425

4

Beta strand

429 – 438

10

Helix

441 – 449

9

Beta strand

455 – 460

6

Helix

464 – 471

8

Beta strand

478 – 485

8

Beta strand

494 – 496

3

Helix

500 – 502

3

Beta strand

507 – 509

3

Helix

512 – 516

5

Beta strand

517 – 525

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 20, 2010. Version 5. Checksum: 05385562F71312B6	FASTA	539	58,487
	10 20 30 40 50 60 MWRLPRALCV HAAKTSKLSG PWSRPAAFMS TLLINQPQYA WLKELGLREE NEGVYNGSWG 70 80 90 100 110 120 GRGEVITTYC PANNEPIARV RQASVADYEE TVKKAREAWK IWADIPAPKR GEIVRQIGDA 130 140 150 160 170 180 LREKIQVLGS LVSLEMGKIL VEGVGEVQEY VDICDYAVGL SRMIGGPILP SERSGHALIE 190 200 210 220 230 240 QWNPVGLVGI ITAFNFPVAV YGWNNAIAMI CGNVCLWKGA PTTSLISVAV TKIIAKVLED 250 260 270 280 290 300 NKLPGAICSL TCGGADIGTA MAKDERVNLL SFTGSTQVGK QVGLMVQERF GRSLLELGGN 310 320 330 340 350 360 NAIIAFEDAD LSLVVPSALF AAVGTAGQRC TTARRLFIHE SIHDEVVNRL KKAYAQIRVG 370 380 390 400 410 420 NPWDPNVLYG PLHTKQAVSM FLGAVEEAKK EGGTVVYGGK VMDRPGNYVE PTIVTGLGHD 430 440 450 460 470 480 ASIAHTETFA PILYVFKFKN EEEVFAWNNE VKQGLSSSIF TKDLGRIFRW LGPKGSDCGI 490 500 510 520 530 VNVNIPTSGA EIGGAFGGEK HTGGGRESGS DAWKQYMRRS TCTINYSKDL PLAQGIKFQ
	Isoform 2 [UniParc]. Checksum: 08F6F7672C948E2C	FASTA	511	55,366
	10 20 30 40 50 60 MSTLLINQPQ YAWLKELGLR EENEGVYNGS WGGRGEVITT YCPANNEPIA RVRQASVADY 70 80 90 100 110 120 EETVKKAREA WKIWADIPAP KRGEIVRQIG DALREKIQVL GSLVSLEMGK ILVEGVGEVQ 130 140 150 160 170 180 EYVDICDYAV GLSRMIGGPI LPSERSGHAL IEQWNPVGLV GIITAFNFPV AVYGWNNAIA 190 200 210 220 230 240 MICGNVCLWK GAPTTSLISV AVTKIIAKVL EDNKLPGAIC SLTCGGADIG TAMAKDERVN 250 260 270 280 290 300 LLSFTGSTQV GKQVGLMVQE RFGRSLLELG GNNAIIAFED ADLSLVVPSA LFAAVGTAGQ 310 320 330 340 350 360 RCTTARRLFI HESIHDEVVN RLKKAYAQIR VGNPWDPNVL YGPLHTKQAV SMFLGAVEEA 370 380 390 400 410 420 KKEGGTVVYG GKVMDRPGNY VEPTIVTGLG HDASIAHTET FAPILYVFKF KNEEEVFAWN 430 440 450 460 470 480 NEVKQGLSSS IFTKDLGRIF RWLGPKGSDC GIVNVNIPTS GAEIGGAFGG EKHTGGGRES 490 500 510 GSDAWKQYMR RSTCTINYSK DLPLAQGIKF Q
	Isoform 3 [UniParc]. Checksum: 257FE6E3EE6C0387	FASTA	347	37,409
	10 20 30 40 50 60 MWRLPRALCV HAAKTSKLSG PWSRPAAFMS TSLISVAVTK IIAKVLEDNK LPGAICSLTC 70 80 90 100 110 120 GGADIGTAMA KDERVNLLSF TGSTQVGKQV GLMVQERFGR SLLELGGNNA IIAFEDADLS 130 140 150 160 170 180 LVVPSALFAA VGTAGQRCTT ARRLFIHESI HDEVVNRLKK AYAQIRVGNP WDPNVLYGPL 190 200 210 220 230 240 HTKQAVSMFL GAVEEAKKEG GTVVYGGKVM DRPGNYVEPT IVTGLGHDAS IAHTETFAPI 250 260 270 280 290 300 LYVFKFKNEE EVFAWNNEVK QGLSSSIFTK DLGRIFRWLG PKGSDCGIVN VNIPTSGAEI 310 320 330 340 GGAFGGEKHT GGGRESGSDA WKQYMRRSTC TINYSKDLPL AQGIKFQ
	Isoform 4 [UniParc]. Checksum: 031B6A8D8BB67F5A	FASTA	502	53,987
	10 20 30 40 50 60 MGSPGRGAGL YFSSSQGLGL IPSPGLSMWR LPRALCVHAA KTSKLSGPWS RPAAFMSTLL 70 80 90 100 110 120 INQPQYAWLK ELGLREENEG VYNGSWGGRG EVITTYCPAN NEPIARVRQA SVADYEETVK 130 140 150 160 170 180 KAREAWKIWA DIPAPKRGEI VRQIGDALRE KIQVLGSLVS LEMGKILVEG VGEVQEYVDI 190 200 210 220 230 240 CDYAVGLSRM IGGPILPSER SGHALIEQWN PVGLVGIITA FNFPVAVYGW NNAIAMICGN 250 260 270 280 290 300 VCLWKGAPTT SLISVAVTKI IAKVLEDNKL PGAICSLTCG GADIGTAMAK DERVNLLSFT 310 320 330 340 350 360 GSTQVGKQVG LMVQERFGRS LLELGGNNAI IAFEDADLSL VVPSALFAAV GTAGQRCTTA 370 380 390 400 410 420 RRLVMDRPGN YVEPTIVTGL GHDASIAHTE TFAPILYVFK FKNEEEVFAW NNEVKQGLSS 430 440 450 460 470 480 SIFTKDLGRI FRWLGPKGSD CGIVNVNIPT SGAEIGGAFG GEKHTGGGRE SGSDAWKQYM 490 500 RRSTCTINYS KDLPLAQGIK FQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Homology between a human protein and a protein of the green garden pea." Lee P., Kuhl W., Gelbart T., Kamimura T., West C., Beutler E. Genomics 21:371-378(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY. Tissue: Kidney, Liver and Placenta.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4). Tissue: Brain, Caudate nucleus and Hippocampus.
[3]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-439. Tissue: Placenta and Uterus.
[5]	"An ancient conserved gene expressed in the human inner ear: identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1)." Skvorak A.B., Robertson N.G., Yin Y., Weremowicz S., Her H., Bieber F.R., Beisel K.W., Lynch E.D., Beier D.R., Morton C.C. Genomics 46:191-199(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 233-268, TISSUE SPECIFICITY.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress." Brocker C., Lassen N., Estey T., Pappa A., Cantore M., Orlova V.V., Chavakis T., Kavanagh K.L., Oppermann U., Vasiliou V. J. Biol. Chem. 285:18452-18463(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 30-526, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION.
[8]	"Mutations in antiquitin in individuals with pyridoxine-dependent seizures." Mills P.B., Struys E., Jakobs C., Plecko B., Baxter P., Baumgartner M., Willemsen M.A.A.P., Omran H., Tacke U., Uhlenberg B., Weschke B., Clayton P.T. Nat. Med. 12:307-309(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PDE VAL-199 AND GLN-427, FUNCTION.
[9]	"Biochemical and molecular characterization of 18 patients with pyridoxine-dependent epilepsy and mutations of the antiquitin (ALDH7A1) gene." Plecko B., Paul K., Paschke E., Stoeckler-Ipsiroglu S., Struys E., Jakobs C., Hartmann H., Luecke T., di Capua M., Korenke C., Hikel C., Reutershahn E., Freilinger M., Baumeister F., Bosch F., Erwa W. Hum. Mutat. 28:19-26(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PDE VAL-202; GLU-291; ILE-301; GLN-335; GLY-395; GLN-427 AND ASN-458.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S74728 mRNA. Translation: AAB31966.1.
AK312459 mRNA. Translation: BAG35366.1. Different initiation.
AK295526 mRNA. Translation: BAG58439.1.
AK297365 mRNA. Translation: BAG59812.1.
AC093535 Genomic DNA. No translation available.
AC099513 Genomic DNA. No translation available.
BC002515 mRNA. Translation: AAH02515.3. Different initiation.
BC071712 mRNA. Translation: AAH71712.1. Different initiation.
BC073174 mRNA. Translation: AAH73174.1. Different initiation.
AF002696 Genomic DNA. Translation: AAC51935.1. Sequence problems.

IPI

IPI00221234.
IPI00909694.
IPI00910420.
IPI00936002.

PIR

A54676.

RefSeq

NP_001173.2. NM_001182.4.
NP_001188306.1. NM_001201377.1.
NP_001189333.1. NM_001202404.1.

UniGene

Hs.483239.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2J6L	X-ray	1.30	A/B/C/D/E/F/G/H	29-527	[»]

ProteinModelPortal

P49419.

SMR

P49419. Positions 30-527.

ModBase

Search...

Protein-protein interaction databases

IntAct

P49419. 4 interactions.

MINT

MINT-1421491.

STRING

9606.ENSP00000387123.

PTM databases

PhosphoSite

P49419.

Polymorphism databases

DMDM

294862544.

2D gel databases

UCD-2DPAGE

P49419.

Proteomic databases

PaxDb

P49419.

PRIDE

P49419.

Protocols and materials databases

DNASU

501.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000409134; ENSP00000387123; ENSG00000164904.
ENST00000447989; ENSP00000414132; ENSG00000164904.

GeneID

501.

KEGG

hsa:501.

UCSC

uc003ktx.3. human.

Organism-specific databases

CTD

501.

GeneCards

GC05M125908.

HGNC

HGNC:877. ALDH7A1.

HPA

HPA023296.

MIM

107323. gene.
266100. phenotype.

neXtProt

NX_P49419.

Orphanet

3006. Pyridoxine-dependent epilepsy.

PharmGKB

PA24704.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1012.

HOGENOM

HOG000271511.

HOVERGEN

HBG050485.

InParanoid

P49419.

KO

K14085.

OMA

VQEYVDV.

OrthoDB

EOG4W3SMQ.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P49419.

UniPathway

UPA00529; UER00386.

Gene expression databases

ArrayExpress

P49419.

Bgee

P49419.

CleanEx

HS_ALDH7A1.

Genevestigator

P49419.

GermOnline

ENSG00000164904. Homo sapiens.

Family and domain databases

Gene3D

3.40.309.10. 1 hit.
3.40.605.10. 1 hit.

InterPro

IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]

Pfam

PF00171. Aldedh. 1 hit.
[Graphical view]

SUPFAM

SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.

PROSITE

PS00070. ALDEHYDE_DEHYDR_CYS. False negative.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ALDH7A1. human.

DrugBank

DB00157. NADH.
DB00165. Pyridoxine.

EvolutionaryTrace

P49419.

GenomeRNAi

501.

NextBio

2097.

SOURCE

Search...

Entry information

Entry name

AL7A1_HUMAN

Accession

Primary (citable) accession number: P49419
Secondary accession number(s): B2R669 , B4DIC7, B4DMA0, E7EPT3, O14619, Q6IPU8, Q9BUL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	April 20, 2010
Last modified:	May 1, 2013
This is version 139 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.