ID L0WFL8_9GAMM Unreviewed; 761 AA.
AC L0WFL8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Acid resistance protein YdeP {ECO:0000313|EMBL:EKF74615.1};
GN ORFNames=A11A3_07343 {ECO:0000313|EMBL:EKF74615.1};
OS Alcanivorax hongdengensis A-11-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=1177179 {ECO:0000313|EMBL:EKF74615.1, ECO:0000313|Proteomes:UP000010164};
RN [1] {ECO:0000313|EMBL:EKF74615.1, ECO:0000313|Proteomes:UP000010164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-11-3 {ECO:0000313|EMBL:EKF74615.1,
RC ECO:0000313|Proteomes:UP000010164};
RX PubMed=23209226; DOI=10.1128/JB.01849-12;
RA Lai Q., Shao Z.;
RT "Genome Sequence of the Alkane-Degrading Bacterium Alcanivorax
RT hongdengensis Type Strain A-11-3.";
RL J. Bacteriol. 194:6972-6972(2012).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:EKF74615.1}.
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DR EMBL; AMRJ01000009; EKF74615.1; -; Genomic_DNA.
DR RefSeq; WP_008928649.1; NZ_AMRJ01000009.1.
DR AlphaFoldDB; L0WFL8; -.
DR STRING; 1177179.A11A3_07343; -.
DR PATRIC; fig|1177179.3.peg.1475; -.
DR eggNOG; COG0243; Bacteria.
DR OrthoDB; 5287431at2; -.
DR Proteomes; UP000010164; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR CDD; cd02787; MopB_CT_ydeP; 1.
DR CDD; cd02767; MopB_ydeP; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037951; MopB_CT_YdeP.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR InterPro; IPR041953; YdeP_MopB.
DR NCBIfam; TIGR01701; Fdhalpha-like; 1.
DR PANTHER; PTHR43105:SF4; PROTEIN YDEP; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF000144; CbbBc; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 113..486
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 641..748
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 761 AA; 83733 MW; D5BDD90B3505D48E CRC64;
MADRRKVPGV KEYGGPAGGW GALKATAEAV HEQMQATQVP GTLLRTNQPG GFDCPGCAWP
DKEHKSTFQF CENGAKAVTW EATKKRVTPA FFAEHTVTEL LAWHDHDLED QGRLTQPMVY
NRATDKYEPI EWQDAFDRIG ETLRTLAPNQ VEFYTSGRAS NEAAYLYQLF ARELGTNNFP
DCSNMCHEPT SVGLPRSIGI GKGTVSLEDF DHCELVLSIG HNPGTNHPRM MGTLHEVSRR
KVPIMVFNPL KERSLERFAD PQNMIEMATF RSTPIASSYF QVRAGGDAAA LKGIMKGVLQ
LEAEGGGVLD REFIDNHTHG YDALAADIHA TGWPDIERES GLKRQDLEMV AAAYARSKAT
IICYGMGITQ HNKGTSNVRL ICDLLLLRGN IGKPGAGICP LRGHSNVQGN RTVGITEKPT
PAFLKNLQDT FGFTPPAEHG HDAVKTMQAM LEGSARALLC LGGNFAVAMP DSERSYPAMK
KLDLSVQVAT KLNRSHLLVA KNSFLFPCLG RTELDMQESG PQSVTVEDSM SMVHASAGKL
PPASSWLKSE PAIVAGMAQS TLPDSKVDWS ALVADYDGIR DLIEKTIPGF ERYNERIRVP
GGFRMPLPAT ERVWNTASGK AEFFVFDGLQ ENRDVPGEDI LRLITVRSHD QYNTTIYGMD
DRYRGVFGRR DVLFMNAEDM AERGLVHGDK VDIETALDGS TLRYDNLTAI EYSVARGTVA
AYYPEANRLV PLDYNDKESG TPSYKSVPVR IIKSVSEAPP A
//
