GenomeNet

Database: UniProt
Entry: E7EQL6_HUMAN
LinkDB: E7EQL6_HUMAN
Original site: E7EQL6_HUMAN 
ID   E7EQL6_HUMAN            Unreviewed;       492 AA.
AC   E7EQL6;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Proline dehydrogenase {ECO:0000256|RuleBase:RU364054};
DE            EC=1.5.5.2 {ECO:0000256|RuleBase:RU364054};
GN   Name=PRODH {ECO:0000313|Ensembl:ENSP00000410805.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000410805.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000410805.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [2] {ECO:0000313|Ensembl:ENSP00000410805.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC       {ECO:0000256|RuleBase:RU364054}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a
CC         quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:132124; EC=1.5.5.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000978,
CC         ECO:0000256|RuleBase:RU364054};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU364054};
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00004739}.
CC   -!- SIMILARITY: Belongs to the proline oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005869, ECO:0000256|RuleBase:RU364054}.
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DR   EMBL; AC007326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IntAct; E7EQL6; 6.
DR   ProteomicsDB; 17596; -.
DR   Antibodypedia; 22803; 352 antibodies from 33 providers.
DR   Ensembl; ENST00000334029.6; ENSP00000334726.2; ENSG00000100033.17.
DR   Ensembl; ENST00000420436.5; ENSP00000410805.1; ENSG00000100033.17.
DR   UCSC; uc002zol.5; human.
DR   HGNC; HGNC:9453; PRODH.
DR   VEuPathDB; HostDB:ENSG00000100033; -.
DR   GeneTree; ENSGT00390000006265; -.
DR   HOGENOM; CLU_018202_3_1_1; -.
DR   OMA; HTWVNAE; -.
DR   ChiTaRS; PRODH; human.
DR   Proteomes; UP000005640; Chromosome 22.
DR   Bgee; ENSG00000100033; Expressed in skin of leg and 97 other cell types or tissues.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006562; P:proline catabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.220; -; 2.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR002872; Proline_DH_dom.
DR   InterPro; IPR015659; Proline_oxidase.
DR   PANTHER; PTHR13914:SF0; PROLINE DEHYDROGENASE 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13914; PROLINE OXIDASE; 1.
DR   Pfam; PF01619; Pro_dh; 1.
DR   SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
PE   1: Evidence at protein level;
KW   FAD {ECO:0000256|RuleBase:RU364054};
KW   Flavoprotein {ECO:0000256|RuleBase:RU364054};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU364054};
KW   Proline metabolism {ECO:0000256|ARBA:ARBA00023062,
KW   ECO:0000256|RuleBase:RU364054};
KW   Proteomics identification {ECO:0007829|EPD:E7EQL6,
KW   ECO:0007829|MaxQB:E7EQL6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT   DOMAIN          152..467
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   REGION          45..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  56255 MW;  028DCBDD68722065 CRC64;
     MKMTFYGHFV AGEDQESIQP LLRHYRAFGV SAILDYGVEE DLSPEEAEHK EMESCTSAAE
     RDGSGTNKRD KQYQAHWAFG DRRNGVISAR TYFYANEAKC DSHMETFLRC IEASGRVSDD
     GFIAIKLTAL GRPQFLLQFS EVLAKWRCFF HQMAVEQGQA GLAAMDTKLE VAVLQESVAK
     LGIASRAEIE DWFTAETLGV SGTMDLLDWS SLIDSRTKLS KHLVVPNAQT GQLEPLLSRF
     TEEEELQMTR MLQRMDVLAK KATEMGVRLM VDAEQTYFQP AISRLTLEMQ RKFNVEKPLI
     FNTYQCYLKD AYDNVTLDVE LARREGWCFG AKLVRGAYLA QERARAAEIG YEDPINPTYE
     ATNAMYHRCL DYVLEELKHN AKAKVMVASH NEDTVRFALR RMEELGLHPA DHRVYFGQLL
     GMCDQISFPL GQAGYPVYKY VPYGPVMEVL PYLSRRALEN SSLMKGTHRE RQLLWLELLR
     RLRTGNLFHR PA
//
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