ID A0A2K5M772_CERAT Unreviewed; 517 AA.
AC A0A2K5M772;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Proline dehydrogenase {ECO:0000256|RuleBase:RU364054};
DE EC=1.5.5.2 {ECO:0000256|RuleBase:RU364054};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000021016.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000021016.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K5M772; -.
DR Ensembl; ENSCATT00000045216.1; ENSCATP00000021016.1; ENSCATG00000034204.1.
DR GeneTree; ENSGT00390000006265; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000034204; Expressed in liver and 8 other cell types or tissues.
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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT DOMAIN 163..489
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT REGION 43..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 59025 MW; 3333D7FBCF728209 CRC64;
MKMTFYGHFV AGEDQESIQP LLRHNRAFGV GAILDYGVEE DLSPEEAEHK EMESCTSAAE
RDGSGTNKRD KQYQAHRAFG DRRSGVISAR TYFYANEAKC DSHMETFLRC IEASGRVSDD
GFIAIKLTAL GRPQFLLQFS EVLTKWRRFF HQMAAEQGKA GLAAMDTKLE VAALQESVAK
MGIASKAEIE DWFTAETLGV SGTVDLLDWG SLIDSRTKLS KHLVVPNAQT GQLEPLLSRF
TEEEELQMTR MLQRMDVLAK KATEVGVRLM VDAEQTYFQP AISRLTLEMQ RKFNVEKPLI
FNTYQCYLKD AYDNVTLGVE LARRECWCFG AKLVRGAYLA QERARAAEIG YEDPINPTYE
ATNAMYHRCL DYVLEELKHN TKAKVMVASH NEDTVRFTLR RMEELCLHPA DHQVYFGQLL
GMCDQISFPL GEWGPPWCDG VRCWAWISWH ICPLAGQAGY PVYKYVPYGP VMEVLPYLSR
RALENSSLMK GARRERQLLW LELLRRLRTG NLFRRPA
//
