ID A0A1M7HH15_9RHOB Unreviewed; 1246 AA.
AC A0A1M7HH15;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Respiratory nitrate reductase alpha subunit apoprotein {ECO:0000313|EMBL:SHM27796.1};
GN ORFNames=SAMN05444389_10692 {ECO:0000313|EMBL:SHM27796.1};
OS Paracoccus solventivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=53463 {ECO:0000313|EMBL:SHM27796.1, ECO:0000313|Proteomes:UP000184444};
RN [1] {ECO:0000313|EMBL:SHM27796.1, ECO:0000313|Proteomes:UP000184444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6637 {ECO:0000313|EMBL:SHM27796.1,
RC ECO:0000313|Proteomes:UP000184444};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FRCK01000006; SHM27796.1; -; Genomic_DNA.
DR RefSeq; WP_073066495.1; NZ_FRCK01000006.1.
DR AlphaFoldDB; A0A1M7HH15; -.
DR STRING; 53463.SAMN05444389_10692; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000184444; Unassembled WGS sequence.
DR GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0042126; P:nitrate metabolic process; IEA:InterPro.
DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR CDD; cd02750; MopB_Nitrate-R-NarG-like; 1.
DR Gene3D; 3.40.50.12440; -; 1.
DR Gene3D; 4.10.1200.10; nitrate reductase tail; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR006468; NarG.
DR InterPro; IPR028189; Nitr_red_alph_N.
DR InterPro; IPR044906; Nitr_red_alph_N_sf.
DR NCBIfam; TIGR01580; narG; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR PANTHER; PTHR43105:SF2; RESPIRATORY NITRATE REDUCTASE 2 ALPHA CHAIN; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF14710; Nitr_red_alph_N; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_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}.
FT DOMAIN 44..108
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1246 AA; 139785 MW; ADD1F48B018E736C CRC64;
MSHLLNRLNF LQSKNVETFS DGHGQVTRES RDWEDTYRNR WRHDKIVRST HGVNCTGSCS
WKIYVKSGIV TWETQQTDYP RTRPDLPNHE PRGCARGASY SWYLYSANRV KNPLVRGRLM
KVWREMRQTM TPIQAWTRIQ SDPILRQSYV ETRGRGGFVR ASWDEATEIV AAANAYTART
YGPDRVFGFS PIPAMSMISY AAGSRYLSLM GGVCMSFYDW YCDLPPASPM TWGEQTDVPE
SADWYNAGYL LLWGSNVPQT RTPDAHFYTE VRYKGTKSAV ICPDYSEAAK FGDVWLNAKQ
GTDAALAMAF GHVILREFHL DRQAEYFEEY CRKYSDFPML VRLDEQDGRL VPGRFLRADD
LDGKLGESNN PEWKTVAIDE RSGGLVAPNG SIGYRWGEAG EWNLEEKAAG AETSLRMSLV
LDGDHDEIAG VDFPYFGGDA VGQFATDADH PDVLTRNIPV RTIRTPSGEV KVATVFDLFC
ANYGLDRGLG GRWVTSSYDD DMPGTPAWAE RITGVARDKI IHVAREFASN AEKTRGKSMI
IIGAAMNHWF HMDMNYRGVI NMLVMCGCVG QSGGGWAHYV GQEKLRPQTG WQPLAFALDW
NRPPRHMNAT SAWYAHTDQW RYETLTADDI LSPTAPAGDW DISLIDYNIR AERMGWLPSA
PQLKTNPLEV ARAAKASGKE IAAYVAEELK SGRLELSCED PDDPANWPRN LFVWRSNLLG
SSGKGHEYFL KHLLGTDHGV LGRDLGEEGG QLPKEARWHQ DGPRGKLDLL VTIDFRMSTT
CVYSDIVLPT ASWYEKDDLN TSDMHPFIHP LQAAVDPAYE SKSDWEIFKA IARKFSEVAP
EILGVETDIV ALPTLHDTPG ELAQDQVRDW KKGECDLIPG KTAPAFIAVE RDFAAVYERF
TSLGPLLDKL GNGGKGISWD TQTEIDNLKD LNGVKADGPA KGRPIIDTAI DAAEVILMLA
PETNGEVAVK AWEALEKATG RHHAHLAEGE HHNKIRFRDI AAQPRKIISS PTWSGIESEK
VSYNAGYTNV HELIPWRTLT GRQQLYQDHL WMRAFGEGFM SYRPPVDLKT VTAEINHEAR
DGEPHVVLNF ITPHQKWGIH STYSDNLLML TLNRGGPVIW ISENDARTAG IVDNDWVELY
NVNGALTARA VVSQRMKDGT TFMYHAQEKI VNTPGSEKTG KRGGIHNSVT RTVLKPTHMI
GGYAQQSYGF NYYGTVGANR DEFVIVRKMK KVDWLDQPAT RKEAAE
//
