ID D0SWG5_ACILW Unreviewed; 536 AA.
AC D0SWG5;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Nitrite reductase [NAD(P)H], small subunit {ECO:0000313|EMBL:EEY89762.1};
DE EC=1.7.1.4 {ECO:0000313|EMBL:EEY89762.1};
GN Name=nirD {ECO:0000313|EMBL:EEY89762.1};
GN ORFNames=HMPREF0017_01639 {ECO:0000313|EMBL:EEY89762.1};
OS Acinetobacter lwoffii SH145.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=575588 {ECO:0000313|EMBL:EEY89762.1, ECO:0000313|Proteomes:UP000018425};
RN [1] {ECO:0000313|Proteomes:UP000018425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH145 {ECO:0000313|Proteomes:UP000018425};
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442}.
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DR EMBL; GG705060; EEY89762.1; -; Genomic_DNA.
DR RefSeq; WP_004280358.1; NZ_GG705060.1.
DR AlphaFoldDB; D0SWG5; -.
DR eggNOG; COG1251; Bacteria.
DR HOGENOM; CLU_003291_4_4_6; -.
DR Proteomes; UP000018425; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-EC.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd03529; Rieske_NirD; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR012748; Rieske-like_NirD.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR041575; Rubredoxin_C.
DR NCBIfam; TIGR02378; nirD_assim_sml; 1.
DR PANTHER; PTHR43429:SF3; NADH OXIDASE-RELATED; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF13806; Rieske_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51300; NIRD; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000313|EMBL:EEY89762.1}.
FT DOMAIN 13..114
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 536 AA; 59562 MW; 77208684EB45E511 CRC64;
MTILKDMNEL NWYEVCNLDE ITPNTGVAAL IEDQQIAIFR VGQEQRVYAL SNQDPFSLAN
VMARGILGDL QGERVVASPI YKQHFSLVTG RCLEEQEQKL LVFPTRIENG KVLVSPTPQK
TYISSNGQNT ERLKLVLIGN GLAGMRCLED LLDMAPDRYD ITVIGEEPWG NYNRIMLSPV
LSGEKSFAEI MLHSADWYAE KGIRFIAGDA AIAIDRSRKQ VHTQKGEVVA YDRLILATGS
KPFMPPIPGA ELEGVISFRD IQDVNRMLDY CKTKQNAVVI GGGLLGLEAA YGLKQQGMNV
TVLHLMDRIM DRQLDMKASQ MLKKSIEDKG IRIITEANTE ELLGIDGHVT QLRLKDGTVL
DADLVVFAVG IRPNKTLAEQ AGLRCNRGVL VNDTMQTYDP SIYAVGECIE HRGQTFGLVE
PLWGQAFICA THLAEHGRLT FKAPTVPTQL KVSGCDVFSA GNFEPQDDFE DIVLNDEKRQ
IYKRIIIQQD KVIGAVLFGD TEDGAWYAEL IADQTPISNI RSKLLFGRDF ALKKAG
//
