ID A0A0Q9S2G4_9BACL Unreviewed; 702 AA.
AC A0A0Q9S2G4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Nitrite reductase {ECO:0000313|EMBL:KRF18662.1};
GN ORFNames=ASG93_11550 {ECO:0000313|EMBL:KRF18662.1};
OS Paenibacillus sp. Soil787.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF18662.1, ECO:0000313|Proteomes:UP000051948};
RN [1] {ECO:0000313|EMBL:KRF18662.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF18662.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF18662.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF18662.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- 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:KRF18662.1}.
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DR EMBL; LMSP01000034; KRF18662.1; -; Genomic_DNA.
DR RefSeq; WP_056836519.1; NZ_LMSP01000034.1.
DR AlphaFoldDB; A0A0Q9S2G4; -.
DR STRING; 1736411.ASG93_11550; -.
DR Proteomes; UP000051948; Unassembled WGS sequence.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00508; MopB_CT_Fdh-Nap-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 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.
PE 4: Predicted;
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 9..67
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 702 AA; 77436 MW; 8ACFFF92A8C60C90 CRC64;
MKSALLTLPK EQPSSHCCFC SMQCGLEIMP SEKTSGLTIK PSPNFPVATS RLCQKGLNAL
DHVLHTDRIL EPLSKEIGEP RRWRTVSWDH AFADIAERIQ GLQATYGPDA IGVYGGGSLT
NEVSYLLGKF TRVALRSKYI DYNGRYCMSS AAAASNQAFG IDRGMTMPLT EIPNAKYIIL
AGTNIAECQP TMMPYLLEAK KKGAVIVTID PRNTMTSKVA DIHVRLQPGF DSVFINGLLH
VMVEEKLVHN RFIEERTVGF EQLKEAVKPF TPARVEELTG ILEAVTRTIA RGFAKAETGI
VLTARGLEQQ VNGVENTLNY INLALITGKI GRKGCGYGAV TGQANGQGGR EHGQKADQLP
GYRLIEDPAA REHVAKVWGI DPNELPGKGV SAYELLQKID EGEIKALIVL GSNPLVSSPN
NRMVERALQK LELLVVVDMF ETETARYAHY LLPGSSFAEA EGTMTNLEGR VFHRQKAMEL
PGNSRLDFHI ICQLADALGR GAYFQYAGIE DVFRELAAAT AGGKADYSGI TYERLQEEKG
IFWPCPAVDH PGTPLLFENH FNHSDGKARL FGIQPKMPAE PIDSDYPFVL TTGRLANHYL
SGAQTRRTEA LNKKAPVPVA EIHPWLAKRI GLSMDNKIRL TSRRGSLIFE VKVTEGIQPR
TVFVPFHWGD EHSINVLTND ALDPTSRMPE FKICAVKVER VE
//
