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Database: UniProt
Entry: A0A0M2S7E1_9ACTN
LinkDB: A0A0M2S7E1_9ACTN
Original site: A0A0M2S7E1_9ACTN 
ID   A0A0M2S7E1_9ACTN        Unreviewed;       306 AA.
AC   A0A0M2S7E1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695};
DE            EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695};
GN   ORFNames=LQ51_02195 {ECO:0000313|EMBL:KKK07485.1};
OS   Micromonospora sp. HK10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1538294 {ECO:0000313|EMBL:KKK07485.1, ECO:0000313|Proteomes:UP000034330};
RN   [1] {ECO:0000313|EMBL:KKK07485.1, ECO:0000313|Proteomes:UP000034330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK10 {ECO:0000313|EMBL:KKK07485.1,
RC   ECO:0000313|Proteomes:UP000034330};
RA   Talukdar M., Das D., Borah C., Deka Boruah H.P., Bora T.C., Singh A.K.;
RT   "Draft genome sequence of Micromonospora HK10, isolated from Kaziranga
RT   National park, Assam, India.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000196-2};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000196-2};
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKK07485.1}.
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DR   EMBL; JTGL01000018; KKK07485.1; -; Genomic_DNA.
DR   RefSeq; WP_046564434.1; NZ_KQ058760.1.
DR   AlphaFoldDB; A0A0M2S7E1; -.
DR   STRING; 1538294.LQ51_02195; -.
DR   PATRIC; fig|1538294.3.peg.2089; -.
DR   HOGENOM; CLU_061158_0_1_11; -.
DR   OrthoDB; 9773461at2; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000034330; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.220; -; 1.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR008219; PRODH_bac_arc.
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   PIRSF; PIRSF000196; Pro_dehydrog; 1.
DR   SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|PIRSR:PIRSR000196-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000196-2};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000196-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          42..297
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT   BINDING         133
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         161
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         185..187
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         224..225
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-2"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000196-1"
SQ   SEQUENCE   306 AA;  33962 MW;  203FEC7716DDDBFF CRC64;
     MLRSVILAAS RSSQVERLVA TAPFTRDVVR RFVAGAGTDD ALRATRVLVD DGQAVTLDYL
     GEDTTTPEQA NATRDEYLAL LRLLAAAKLT PAAEVSVKLS ALGQLFDEQL AYDNARAICA
     AADAAGTTVT LDMEDHTTTD STLDVLAKLR KDYPSTGAVL QAYLRRTESD CRELSGAGSR
     VRLCKGAYSE PESVAYQSAR EVDKSYVRCM NVLMSGDGYP MLATHDPRLI AIGEDRARWF
     DRDPDRFEFQ MLYGIRPEEQ KRLIGEGYTV RTYVPYGDQW YGYLMRRLAE RPANLVFFGR
     ALASKK
//
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