P54886 (P5CS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Delta-1-pyrroline-5-carboxylate synthase
Short name=P5CS

Alternative name(s):
Aldehyde dehydrogenase family 18 member A1

Including the following 2 domains:

1. Glutamate 5-kinase
   Short name=GK
   EC=2.7.2.11
   Alternative name(s):
   Gamma-glutamyl kinase
2. Gamma-glutamyl phosphate reductase
   Short name=GPR
   EC=1.2.1.41
   Alternative name(s):
   Glutamate-5-semialdehyde dehydrogenase
   Glutamyl-gamma-semialdehyde dehydrogenase

Gene names

Name:	ALDH18A1
Synonyms:	GSAS, P5CS, PYCS

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	795 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + L-glutamate = ADP + L-glutamate 5-phosphate. L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH.
Enzyme regulation	Isoform Short is inhibited by L-ornithine with a Ki of approximately 0.25 mm. Isoform Long is insensitive to ornithine inhibition. This is due to the two amino acid insert which abolishes feedback inhibition of P5CS activity by L-ornithine. Ref.2
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular location	Mitochondrion inner membrane.
Involvement in disease	Defects in ALDH18A1 are the cause of mental retardation-joint hypermobility-skin laxity with or without metabolic abnormalities (MRJHSL) [MIM:612652]. Clinical manifestations include microcephaly, progressive neurologic dysfunction, mental retardation, progeroid appearance, joint hypermobility, skin laxity and hyperelasticity, cataracts. Some patients manifest metabolic disturbances such as hyperammonemia, hypoornithinemia, hypocitrullinemia, hypoargininemia and hypoprolinemia. Ref.8 Ref.9
Sequence similarities	In the N-terminal section; belongs to the glutamate 5-kinase family. In the C-terminal section; belongs to the gamma-glutamyl phosphate reductase family.
Sequence caution	The sequence BAH12086.1 differs from that shown. Reason: Erroneous initiation. The sequence BAH13064.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Proline biosynthesis
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Mental retardation
Ligand	ATP-binding NADP Nucleotide-binding
Molecular function	Kinase Oxidoreductase Transferase
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	proline biosynthetic process Traceable author statement. Source: ProtInc
Cellular component	mitochondrial inner membrane Traceable author statement. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate 5-kinase activity Inferred from electronic annotation. Source: EC glutamate-5-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P54886-1)

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 Short (identifier: P54886-2)

The sequence of this isoform differs from the canonical sequence as follows:
     239-240: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 795

795

Delta-1-pyrroline-5-carboxylate synthase

PRO_0000109769

Regions

Region

1 – 361

361

Glutamate 5-kinase

Region

362 – 795

434

Gamma-glutamyl phosphate reductase

Natural variations

Alternative sequence

239 – 240

2

Missing in isoform Short.

VSP_005215

Natural variant

84

1

R → Q in MRJHSL; with metabolic disturbances; reduction of activity. Ref.8

VAR_038482

Natural variant

299

1

T → I. Ref.3 Ref.6
Corresponds to variant rs2275272 [ dbSNP | Ensembl ].

VAR_051792

Natural variant

372

1

S → Y. Ref.6
Corresponds to variant rs3765571 [ dbSNP | Ensembl ].

VAR_051793

Natural variant

784

1

H → Y in MRJHSL; without metabolic disturbances; does not affect proline and ornithine biosynthetic activity. Ref.9

VAR_058006

Experimental info

Sequence conflict

87

1

E → K in BAG35201. Ref.3

Sequence conflict

126

1

R → T in CAA64224. Ref.1

Sequence conflict

266

1

S → P in CAA64224. Ref.1

Sequence conflict

299

1

T → P in CAA64224. Ref.1

Sequence conflict

305 – 307

3

MGG → NGC in CAA64224. Ref.1

Sequence conflict

314 – 315

2

AA → ST in CAA64224. Ref.1

Sequence conflict

487 – 493

7

LPQVAAL → PTPGGSF in CAA64224. Ref.1

Secondary structure

1

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795

Helix Strand Turn

Details...

Helix

363 – 379

17

Helix

382 – 398

17

Helix

400 – 414

15

Turn

415 – 417

3

Helix

420 – 424

5

Helix

430 – 446

17

Beta strand

454 – 461

8

Beta strand

464 – 472

9

Beta strand

475 – 482

8

Helix

486 – 497

12

Beta strand

500 – 504

5

Helix

507 – 509

3

Helix

510 – 525

16

Turn

526 – 528

3

Helix

530 – 532

3

Beta strand

533 – 535

3

Beta strand

553 – 559

7

Helix

561 – 570

10

Beta strand

572 – 574

3

Beta strand

584 – 588

5

Turn

594 – 596

3

Helix

597 – 606

10

Beta strand

614 – 621

8

Helix

622 – 624

3

Helix

628 – 639

12

Beta strand

643 – 646

4

Helix

648 – 651

4

Beta strand

670 – 680

11

Helix

681 – 691

11

Beta strand

694 – 700

7

Helix

704 – 713

10

Beta strand

716 – 723

8

Helix

725 – 727

3

Turn

730 – 734

5

Beta strand

745 – 747

3

Helix

754 – 757

4

Beta strand

758 – 769

12

Helix

771 – 774

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 8BF27EF2A8FB2D79	FASTA	795	87,302
	10 20 30 40 50 60 MLSQVYRCGF QPFNQHLLPW VKCTTVFRSH CIQPSVIRHV RSWSNIPFIT VPLSRTHGKS 70 80 90 100 110 120 FAHRSELKHA KRIVVKLGSA VVTRGDECGL ALGRLASIVE QVSVLQNQGR EMMLVTSGAV 130 140 150 160 170 180 AFGKQRLRHE ILLSQSVRQA LHSGQNQLKE MAIPVLEARA CAAAGQSGLM ALYEAMFTQY 190 200 210 220 230 240 SICAAQILVT NLDFHDEQKR RNLNGTLHEL LRMNIVPIVN TNDAVVPPAE PNSDLQGVNV 250 260 270 280 290 300 ISVKDNDSLA ARLAVEMKTD LLIVLSDVEG LFDSPPGSDD AKLIDIFYPG DQQSVTFGTK 310 320 330 340 350 360 SRVGMGGMEA KVKAALWALQ GGTSVVIANG THPKVSGHVI TDIVEGKKVG TFFSEVKPAG 370 380 390 400 410 420 PTVEQQGEMA RSGGRMLATL EPEQRAEIIH HLADLLTDQR DEILLANKKD LEEAEGRLAA 430 440 450 460 470 480 PLLKRLSLST SKLNSLAIGL RQIAASSQDS VGRVLRRTRI AKNLELEQVT VPIGVLLVIF 490 500 510 520 530 540 ESRPDCLPQV AALAIASGNG LLLKGGKEAA HSNRILHLLT QEALSIHGVK EAVQLVNTRE 550 560 570 580 590 600 EVEDLCRLDK MIDLIIPRGS SQLVRDIQKA AKGIPVMGHS EGICHMYVDS EASVDKVTRL 610 620 630 640 650 660 VRDSKCEYPA ACNALETLLI HRDLLRTPLF DQIIDMLRVE QVKIHAGPKF ASYLTFSPSE 670 680 690 700 710 720 VKSLRTEYGD LELCIEVVDN VQDAIDHIHK YGSSHTDVIV TEDENTAEFF LQHVDSACVF 730 740 750 760 770 780 WNASTRFSDG YRFGLGAEVG ISTSRIHARG PVGLEGLLTT KWLLRGKDHV VSDFSEHGSL 790 KYLHENLPIP QRNTN
	Isoform Short [UniParc]. Checksum: 550F0B435805C0CA	FASTA	793	87,089
	10 20 30 40 50 60 MLSQVYRCGF QPFNQHLLPW VKCTTVFRSH CIQPSVIRHV RSWSNIPFIT VPLSRTHGKS 70 80 90 100 110 120 FAHRSELKHA KRIVVKLGSA VVTRGDECGL ALGRLASIVE QVSVLQNQGR EMMLVTSGAV 130 140 150 160 170 180 AFGKQRLRHE ILLSQSVRQA LHSGQNQLKE MAIPVLEARA CAAAGQSGLM ALYEAMFTQY 190 200 210 220 230 240 SICAAQILVT NLDFHDEQKR RNLNGTLHEL LRMNIVPIVN TNDAVVPPAE PNSDLQGVIS 250 260 270 280 290 300 VKDNDSLAAR LAVEMKTDLL IVLSDVEGLF DSPPGSDDAK LIDIFYPGDQ QSVTFGTKSR 310 320 330 340 350 360 VGMGGMEAKV KAALWALQGG TSVVIANGTH PKVSGHVITD IVEGKKVGTF FSEVKPAGPT 370 380 390 400 410 420 VEQQGEMARS GGRMLATLEP EQRAEIIHHL ADLLTDQRDE ILLANKKDLE EAEGRLAAPL 430 440 450 460 470 480 LKRLSLSTSK LNSLAIGLRQ IAASSQDSVG RVLRRTRIAK NLELEQVTVP IGVLLVIFES 490 500 510 520 530 540 RPDCLPQVAA LAIASGNGLL LKGGKEAAHS NRILHLLTQE ALSIHGVKEA VQLVNTREEV 550 560 570 580 590 600 EDLCRLDKMI DLIIPRGSSQ LVRDIQKAAK GIPVMGHSEG ICHMYVDSEA SVDKVTRLVR 610 620 630 640 650 660 DSKCEYPAAC NALETLLIHR DLLRTPLFDQ IIDMLRVEQV KIHAGPKFAS YLTFSPSEVK 670 680 690 700 710 720 SLRTEYGDLE LCIEVVDNVQ DAIDHIHKYG SSHTDVIVTE DENTAEFFLQ HVDSACVFWN 730 740 750 760 770 780 ASTRFSDGYR FGLGAEVGIS TSRIHARGPV GLEGLLTTKW LLRGKDHVVS DFSEHGSLKY 790 LHENLPIPQR NTN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Database cloning human delta 1-pyrroline-5-carboxylate synthetase (P5CS) cDNA: a bifunctional enzyme catalyzing the first 2 steps in proline biosynthesis." Aral B., Schlenzig J.S., Liu G., Kamoun P. C. R. Acad. Sci. III, Sci. Vie 319:171-178(1996) [PubMed: 8761662] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG). Tissue: Kidney.
[2]	"Molecular enzymology of mammalian delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition." Hu C.A., Lin W.-W., Obie C., Valle D. J. Biol. Chem. 274:6754-6762(1999) [PubMed: 10037775] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), ENZYME REGULATION. Tissue: Small intestine.
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANT ILE-299. Tissue: Brain and Hippocampus.
[4]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT), VARIANTS ILE-299 AND TYR-372. Tissue: Brain and Uterus.
[7]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"Hyperammonemia with reduced ornithine, citrulline, arginine and proline: a new inborn error caused by a mutation in the gene encoding delta(1)-pyrroline-5-carboxylate synthase." Baumgartner M.R., Hu C.A., Almashanu S., Steel G., Obie C., Aral B., Rabier D., Kamoun P., Saudubray J.-M., Valle D. Hum. Mol. Genet. 9:2853-2858(2000) [PubMed: 11092761] [Abstract] Cited for: VARIANT MRJHSL GLN-84, CHARACTERIZATION OF VARIANT MRJHSL GLN-84.
[9]	"A missense mutation in ALDH18A1, encoding Delta1-pyrroline-5-carboxylate synthase (P5CS), causes an autosomal recessive neurocutaneous syndrome." Bicknell L.S., Pitt J., Aftimos S., Ramadas R., Maw M.A., Robertson S.P. Eur. J. Hum. Genet. 16:1176-1186(2008) [PubMed: 18478038] [Abstract] Cited for: VARIANT MRJHSL TYR-784, CHARACTERIZATION OF VARIANT MRJHSL TYR-784.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X94453 mRNA. Translation: CAA64224.1.
U76542 mRNA. Translation: AAD17454.1.
U68758 mRNA. Translation: AAD00169.1.
AK295487 mRNA. Translation: BAH12086.1. Different initiation.
AK299557 mRNA. Translation: BAH13064.1. Different initiation.
AK312271 mRNA. Translation: BAG35201.1.
AL356632 Genomic DNA. Translation: CAI16765.1.
AL356632 Genomic DNA. Translation: CAI16766.1.
CH471066 Genomic DNA. Translation: EAW49995.1.
CH471066 Genomic DNA. Translation: EAW49994.1.
CH471066 Genomic DNA. Translation: EAW49996.1.
CH471066 Genomic DNA. Translation: EAW49997.1.
BC106054 mRNA. Translation: AAI06055.1.
BC117240 mRNA. Translation: AAI17241.1.
BC117242 mRNA. Translation: AAI17243.1.
BC143930 mRNA. Translation: AAI43931.1.

IPI

IPI00008982.
IPI00218547.

RefSeq

NP_001017423.1. NM_001017423.1.
NP_002851.2. NM_002860.3.

UniGene

Hs.500645.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2H5G	X-ray	2.25	A/B	362-795	[»]

ProteinModelPortal

P54886.

SMR

P54886. Positions 69-357, 362-794.

ModBase

Search...

Protein-protein interaction databases

IntAct

P54886. 7 interactions.

STRING

P54886.

PTM databases

PhosphoSite

P54886.

Polymorphism databases

DMDM

6226882.

Proteomic databases

PRIDE

P54886.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371224; ENSP00000360268; ENSG00000059573.

GeneID

5832.

KEGG

hsa:5832.

NMPDR

fig|9606.3.peg.4399.

UCSC

uc001kkz.1. human.

Organism-specific databases

CTD

5832.

GeneCards

GC10M097355.

H-InvDB

HIX0201510.

HGNC

HGNC:9722. ALDH18A1.

HPA

HPA008333.
HPA012604.

MIM

138250. gene.
612652. phenotype.

neXtProt

NX_P54886.

Orphanet

168978. Neurocutaneous syndrome, Bicknell type.

PharmGKB

PA34065.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05292.

GeneTree

ENSGT00500000044903.

HOVERGEN

HBG007911.

InParanoid

P54886.

OMA

HVDSACV.

OrthoDB

EOG4ZKJKN.

PhylomeDB

P54886.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-11424.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P54886.

Bgee

P54886.

CleanEx

HS_ALDH18A1.

Genevestigator

P54886.

GermOnline

ENSG00000059573. Homo sapiens.

Family and domain databases

InterPro

IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR000965. G-glutamylP_reductase.
IPR020593. G-glutamylP_reductase_CS.
IPR001057. Glu/AcGlu_kinase.
IPR019797. Glutamate_5-kinase_CS.
IPR005766. P5_carboxy_syn.
[Graphical view]

Gene3D

G3DSA:3.40.1160.10. Aa_kinase. 1 hit.
G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 2 hits.

KO

K12657.

Pfam

PF00696. AA_kinase. 1 hit.
PF00171. Aldedh. 1 hit.
[Graphical view]

PIRSF

PIRSF036429. P5C_syn. 1 hit.

PRINTS

PR00474. GLU5KINASE.

SUPFAM

SSF53633. Aa_kinase. 1 hit.
SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.

TIGRFAMs

TIGR01092. P5CS. 1 hit.
TIGR00407. ProA. 1 hit.

PROSITE

PS00902. GLUTAMATE_5_KINASE. 1 hit.
PS01223. PROA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00142. L-Glutamic Acid.

NextBio

22726.

SOURCE

Search...

Entry information

Entry name

P5CS_HUMAN

Accession

Primary (citable) accession number: P54886
Secondary accession number(s): B2R5Q4 , B7Z350, B7Z5X8, B7ZLP1, D3DR44, O95952, Q3KQU2, Q5T566, Q5T567, Q9UM72

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 30, 2000
Last modified:	January 25, 2012
This is version 129 of the entry and version 2 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.