Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Proline dehydrogenase 1, mitochondrial

Gene

slgA

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts proline to delta-1-pyrroline-5-carboxylate.1 Publication

Catalytic activityi

L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol.

Cofactori

Pathwayi: L-proline degradation into L-glutamate

This protein is involved in step 1 of the subpathway that synthesizes L-glutamate from L-proline.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Proline dehydrogenase 1, mitochondrial (slgA)
  2. no protein annotated in this organism
This subpathway is part of the pathway L-proline degradation into L-glutamate, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from L-proline, the pathway L-proline degradation into L-glutamate and in Amino-acid degradation.

GO - Molecular functioni

  • FAD binding Source: UniProtKB
  • proline dehydrogenase activity Source: FlyBase

GO - Biological processi

  • glutamate biosynthetic process Source: FlyBase
  • locomotory behavior Source: FlyBase
  • phototaxis Source: FlyBase
  • proline catabolic process Source: FlyBase
  • proline catabolic process to glutamate Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Proline metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-DME-70688. Proline catabolism.
UniPathwayiUPA00261; UER00373.

Names & Taxonomyi

Protein namesi
Recommended name:
Proline dehydrogenase 1, mitochondrial (EC:1.5.5.2)
Alternative name(s):
Proline oxidase
Protein sluggish-A
Gene namesi
Name:slgA
Synonyms:slg
ORF Names:CG1417
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0003423. slgA.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: FlyBase
  • mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Flies exhibit reduced proline oxidase activity which produces sluggish behavior.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionSequence analysisAdd
BLAST
Chaini31 – 681651Proline dehydrogenase 1, mitochondrialPRO_0000025803Add
BLAST

Proteomic databases

PaxDbiQ04499.
PRIDEiQ04499.

Expressioni

Tissue specificityi

Most abundant in developing nervous system.1 Publication

Developmental stagei

Expressed in developing embryo as well as in adult.1 Publication

Gene expression databases

BgeeiQ04499.
ExpressionAtlasiQ04499. differential.
GenevisibleiQ04499. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CG10069Q9W2I61EBI-197717,EBI-146309
CG6608Q7K0L71EBI-197717,EBI-190238
Mob4Q7K0E31EBI-197717,EBI-157547

Protein-protein interaction databases

BioGridi59392. 19 interactions.
IntActiQ04499. 5 interactions.
STRINGi7227.FBpp0076903.

Structurei

3D structure databases

ProteinModelPortaliQ04499.
SMRiQ04499. Positions 427-643.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the proline oxidase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0186. Eukaryota.
COG0506. LUCA.
GeneTreeiENSGT00390000006265.
InParanoidiQ04499.
KOiK00318.
OMAiRKEMESC.
OrthoDBiEOG7K9K2J.
PhylomeDBiQ04499.

Family and domain databases

Gene3Di3.20.20.220. 3 hits.
InterProiIPR029041. FAD-linked_oxidoreductase-like.
IPR002872. Proline_DH_dom.
IPR015659. Proline_oxidase.
[Graphical view]
PANTHERiPTHR13914. PTHR13914. 2 hits.
PfamiPF01619. Pro_dh. 1 hit.
[Graphical view]
SUPFAMiSSF51730. SSF51730. 3 hits.

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform D (identifier: Q04499-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MALLRSLSAQ RTAISLVYGR NSSKSSNSVA VAACRSFHQR GSGSTSIAGE
60 70 80 90 100
GAASESTRGV NGARFLHSGD RPLQASTLVQ PEVVSSETVK RSMKQESSQE
110 120 130 140 150
KNPSPAGSPQ RDPLDVSFND PIAAFKSKTT GELIRAYLVY MICSSEKLVE
160 170 180 190 200
HNMTLMKLAR NLLGQKLFVL LMKSSFYGHF VAGENRHTIV PALERLRSFG
210 220 230 240 250
VKPILDYSVE EDITQEEAEK REVESSVSSA GDKKEEGSMP QYHVDKSFAD
260 270 280 290 300
RRYKVSSART YFYLNEATCE RNMEIFIKCL EAVSDDDRKA PRAVATGATF
310 320 330 340 350
GTGITAIKLT ALGRPQLLLQ LSEVIMRTRK YMEDMVGGQG NVLTHHKTIK
360 370 380 390 400
DLEKYYATLG DNKDVKEFLN NVTSDKEGIL HLFPWSGIVD EDSQLSDTFR
410 420 430 440 450
VPDPQTGQMR RLISQIPPKE EEMFRNMIRR LNTIVKAAAD LDVRIMVDAE
460 470 480 490 500
QTYFQPAISR ITLEMMRKYN KDKAIVFNTY QCYLRETFRE VNTDLEQAKR
510 520 530 540 550
QNFYFGAKLV RGAYMDQERD RAKSLGYPDP VNPTFEATTD MYHRTLSECL
560 570 580 590 600
RRIKLMKDCD DDARKIGIMV ASHNEDTVRF AIQQMKEIGI SPEDKVICFG
610 620 630 640 650
QLLGMCDYIT FPLGQAGYSA YKYIPYGPVE EVLPYLSRRA QENKGVLKKI
660 670 680
KKEKRLLLSE IRRRLMRGQL FYKPKGNYVP I
Note: No experimental confirmation available.
Length:681
Mass (Da):77,153
Last modified:August 30, 2005 - v2
Checksum:i2AB69ABB67D83FF8
GO
Isoform A (identifier: Q04499-2) [UniParc]FASTAAdd to basket

Also known as: F

The sequence of this isoform differs from the canonical sequence as follows:
     158-192: LARNLLGQKLFVLLMKSSFYGHFVAGENRHTIVPA → WSKNVLGQRLFTLLMKATFYGHFVAGEDQIKIIPT
     285-296: Missing.

Show »
Length:669
Mass (Da):75,952
Checksum:i89C68093DF0D82EE
GO
Isoform B (identifier: Q04499-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     285-296: Missing.

Note: No experimental confirmation available.
Show »
Length:669
Mass (Da):75,857
Checksum:i976800739C0839CC
GO
Isoform C (identifier: Q04499-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-325: Missing.

Note: No experimental confirmation available.
Show »
Length:356
Mass (Da):41,558
Checksum:iF1A5FF82FD03142C
GO
Isoform E (identifier: Q04499-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     158-192: LARNLLGQKLFVLLMKSSFYGHFVAGENRHTIVPA → WSKNVLGQRLFTLLMKATFYGHFVAGEDQIKIIPT

Note: No experimental confirmation available.
Show »
Length:681
Mass (Da):77,248
Checksum:i783D5C065E1EC77A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421S → N in AAA02748 (PubMed:8096642).Curated
Sequence conflicti147 – 1471K → N in AAA02748 (PubMed:8096642).Curated
Sequence conflicti149 – 1491V → F in AAC28410 (PubMed:9520435).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 325325Missing in isoform C. CuratedVSP_015400Add
BLAST
Alternative sequencei158 – 19235LARNL…TIVPA → WSKNVLGQRLFTLLMKATFY GHFVAGEDQIKIIPT in isoform A and isoform E. 2 PublicationsVSP_015401Add
BLAST
Alternative sequencei285 – 29612Missing in isoform A and isoform B. 2 PublicationsVSP_015402Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07330 mRNA. Translation: AAA02748.1.
AF017777 Genomic DNA. Translation: AAC28410.1.
AE014298 Genomic DNA. Translation: AAF50814.2.
AE014298 Genomic DNA. Translation: AAF50819.2.
AE014298 Genomic DNA. Translation: AAF50820.2.
AE014298 Genomic DNA. Translation: AAF50821.1.
AE014298 Genomic DNA. Translation: AAF50822.3.
AY069407 mRNA. Translation: AAL39552.1.
PIRiA47302.
RefSeqiNP_001245791.1. NM_001258862.2. [Q04499-3]
NP_001245792.1. NM_001258863.2. [Q04499-2]
NP_001245793.1. NM_001258864.2. [Q04499-2]
NP_001245794.1. NM_001258865.2. [Q04499-2]
NP_001245795.1. NM_001258866.2. [Q04499-3]
NP_001245796.1. NM_001258867.2. [Q04499-5]
NP_523433.2. NM_078709.4. [Q04499-5]
NP_728422.1. NM_167751.3. [Q04499-2]
NP_728423.1. NM_167752.3. [Q04499-1]
NP_728424.1. NM_167753.3. [Q04499-3]
NP_728425.1. NM_167754.2. [Q04499-4]
NP_996526.1. NM_206803.3. [Q04499-2]
NP_996527.1. NM_206804.3. [Q04499-2]
NP_996528.1. NM_206805.3. [Q04499-2]
UniGeneiDm.6612.

Genome annotation databases

EnsemblMetazoaiFBtr0077204; FBpp0076903; FBgn0003423. [Q04499-1]
GeneIDi33117.
KEGGidme:Dmel_CG1417.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07330 mRNA. Translation: AAA02748.1.
AF017777 Genomic DNA. Translation: AAC28410.1.
AE014298 Genomic DNA. Translation: AAF50814.2.
AE014298 Genomic DNA. Translation: AAF50819.2.
AE014298 Genomic DNA. Translation: AAF50820.2.
AE014298 Genomic DNA. Translation: AAF50821.1.
AE014298 Genomic DNA. Translation: AAF50822.3.
AY069407 mRNA. Translation: AAL39552.1.
PIRiA47302.
RefSeqiNP_001245791.1. NM_001258862.2. [Q04499-3]
NP_001245792.1. NM_001258863.2. [Q04499-2]
NP_001245793.1. NM_001258864.2. [Q04499-2]
NP_001245794.1. NM_001258865.2. [Q04499-2]
NP_001245795.1. NM_001258866.2. [Q04499-3]
NP_001245796.1. NM_001258867.2. [Q04499-5]
NP_523433.2. NM_078709.4. [Q04499-5]
NP_728422.1. NM_167751.3. [Q04499-2]
NP_728423.1. NM_167752.3. [Q04499-1]
NP_728424.1. NM_167753.3. [Q04499-3]
NP_728425.1. NM_167754.2. [Q04499-4]
NP_996526.1. NM_206803.3. [Q04499-2]
NP_996527.1. NM_206804.3. [Q04499-2]
NP_996528.1. NM_206805.3. [Q04499-2]
UniGeneiDm.6612.

3D structure databases

ProteinModelPortaliQ04499.
SMRiQ04499. Positions 427-643.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59392. 19 interactions.
IntActiQ04499. 5 interactions.
STRINGi7227.FBpp0076903.

Proteomic databases

PaxDbiQ04499.
PRIDEiQ04499.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077204; FBpp0076903; FBgn0003423. [Q04499-1]
GeneIDi33117.
KEGGidme:Dmel_CG1417.

Organism-specific databases

CTDi33117.
FlyBaseiFBgn0003423. slgA.

Phylogenomic databases

eggNOGiKOG0186. Eukaryota.
COG0506. LUCA.
GeneTreeiENSGT00390000006265.
InParanoidiQ04499.
KOiK00318.
OMAiRKEMESC.
OrthoDBiEOG7K9K2J.
PhylomeDBiQ04499.

Enzyme and pathway databases

UniPathwayiUPA00261; UER00373.
ReactomeiR-DME-70688. Proline catabolism.

Miscellaneous databases

GenomeRNAii33117.
PROiQ04499.

Gene expression databases

BgeeiQ04499.
ExpressionAtlasiQ04499. differential.
GenevisibleiQ04499. DM.

Family and domain databases

Gene3Di3.20.20.220. 3 hits.
InterProiIPR029041. FAD-linked_oxidoreductase-like.
IPR002872. Proline_DH_dom.
IPR015659. Proline_oxidase.
[Graphical view]
PANTHERiPTHR13914. PTHR13914. 2 hits.
PfamiPF01619. Pro_dh. 1 hit.
[Graphical view]
SUPFAMiSSF51730. SSF51730. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sluggish-A gene of Drosophila melanogaster is expressed in the nervous system and encodes proline oxidase, a mitochondrial enzyme involved in glutamate biosynthesis."
    Hayward D.C., Delaney S.J., Campbell H.D., Ghysen A., Benzer S., Kasprzak A.B., Cotsell J.N., Young I.G., Miklos G.L.G.
    Proc. Natl. Acad. Sci. U.S.A. 90:2979-2983(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    Strain: Canton-S.
  2. "Data transferability from model organisms to human beings: insights from the functional genomics of the flightless region of Drosophila."
    Maleszka R., de Couet H.G., Miklos G.L.G.
    Proc. Natl. Acad. Sci. U.S.A. 95:3731-3736(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
    Strain: Canton-S.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiPROD_DROME
AccessioniPrimary (citable) accession number: Q04499
Secondary accession number(s): O61349
, Q8IQ45, Q8IQ46, Q8T0C7, Q9VRH7, Q9VRH8, Q9VRH9, Q9VRI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: August 30, 2005
Last modified: June 8, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.