ID A0A195CB49_9HYME Unreviewed; 687 AA.
AC A0A195CB49;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Proline dehydrogenase {ECO:0000256|RuleBase:RU364054};
DE EC=1.5.5.2 {ECO:0000256|RuleBase:RU364054};
GN ORFNames=ALC62_11276 {ECO:0000313|EMBL:KYM97930.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYM97930.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYM97930.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYM97930.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM97930.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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|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; KQ978023; KYM97930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195CB49; -.
DR STRING; 456900.A0A195CB49; -.
DR Proteomes; UP000078542; Unassembled WGS sequence.
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:UP000078542}.
FT DOMAIN 245..656
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT REGION 202..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 77993 MW; FC026EFA897B7C99 CRC64;
MAFLRSVPRR CCAGKKLVKC GASPLAVVGL LENVTAATAT TTAAAATATA AAVTRTPPSL
RLVAQVRGYA TSSSSSAATT DVKQQRQQQQ SAVPRQIDPL DLKFNDPIAS FKSKTTMELM
RAYVVYQMCS VEYLVENNMK VMKMVKSILG EKLFTKLMKA TFYGHFVAGE DEVQITPVLD
RLRQFGVKPI LDYSVEEDIS QEEAERREIQ ASVSEAGDEK REGPLKKYHV EKSFADRRYK
VSSARTYFYL NEASCERNMD IFIRCLEAVA KDEVHTLRLK FPSQNITTHD QADPNPESIF
TGASMGMGIT AVKLTALGRP QLLLQLSEVI MRARQYTSDV IGGEGAVLAH HAKPDDFKKK
FEEARIKDTE VQKFLQKIQS DKEGVIHLFP WSGILDENYE LSETFQVPDI KTGKMVRLMS
QLTSKEEEMF RNMIRRLNNI VTVADSLDVR IMIDAEQTYF QPAISRLTLE MMRKYNTKKA
VVFNTYQTYL QDAFNEVKTD LEQAERQNFY FGAKLVRGAY IEQERARAAA MGYPDPTNPT
FEATTESYHK TLMECLRRMK QYKDKGEDPK KIGIMVASHN EDTVRFAIEK MKEIGISPED
KVICFGQLLG MCDYITFPLG QSGYSAYKYI PYGPVKEVLP YLSRRAQENR GILKKIKKEK
RLLLNEITRR IVRGKLFYKP KGNYTPV
//