ID A3JP30_9RHOB Unreviewed; 1064 AA.
AC A3JP30;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Oxidoreductase, NAD-binding/iron-sulfur cluster-binding protein {ECO:0000313|EMBL:EBA05478.1};
GN ORFNames=RB2150_15351 {ECO:0000313|EMBL:EBA05478.1};
OS Rhodobacteraceae bacterium HTCC2150.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=388401 {ECO:0000313|EMBL:EBA05478.1, ECO:0000313|Proteomes:UP000004731};
RN [1] {ECO:0000313|EMBL:EBA05478.1, ECO:0000313|Proteomes:UP000004731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2150 {ECO:0000313|EMBL:EBA05478.1,
RC ECO:0000313|Proteomes:UP000004731};
RX PubMed=20889754; DOI=10.1128/JB.01088-10;
RA Kang I., Oh H.M., Vergin K.L., Giovannoni S.J., Cho J.C.;
RT "Genome sequence of the marine alphaproteobacterium HTCC2150, assigned to
RT the Roseobacter clade.";
RL J. Bacteriol. 192:6315-6316(2010).
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:EBA05478.1}.
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DR EMBL; AAXZ01000001; EBA05478.1; -; Genomic_DNA.
DR AlphaFoldDB; A3JP30; -.
DR eggNOG; COG1018; Bacteria.
DR eggNOG; COG1600; Bacteria.
DR OrthoDB; 9792185at2; -.
DR Proteomes; UP000004731; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06185; PDR_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR012832; RDH.
DR InterPro; IPR028894; RDH_dom.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR NCBIfam; TIGR02486; RDH; 1.
DR PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF13486; Dehalogenase; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000004731};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 544..574
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 749..851
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 977..1064
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 1064 AA; 117416 MW; 3108D21BC33C17A3 CRC64;
MAKLFSYKNR PMHFGQYPME KLVRQNDMPD LTAIGTPKPL SFRRPDDPLS IVNAMQEYQA
MLDATREGYV KRERADIPSD LQERSDHLKS FGYYCDAAMV GICEIPNTAN LETPLKNPDV
GRLAENLKTM QPKTFAAGVD VIMASLRESM AKPPKDCAHH THALLFLYEY PRDPNQGEVG
TDWIQNAQAP RACLRGMETA VTLANYIRSL GWDARAHSPA ESDVNLDQLA VAAGLATIVG
NHVESPFHGN RFQICAVTTT LEMATDRPLA AKQSLGASWK LGLGTNAKNA RNSDPFRTRN
FADGPHPFER LKRVENPTTY IDAVNVARVP KRANMFARSL FGDLGKKVQD SSKNGNYLRK
SAAAFAFRPS LGAFILLQDG KAGDIHPSTL DPTSNAANIK AALYYLGVDA AGLSACPDWV
YYSHDAAGEP LTPYHSNAIS MIIDQGQETM EGASGDDWIA SAQSMRAYLR FSLLGGVLAQ
HLRRLGYTAR VHTVMDDEVL HPPLLLLAGL GEVSRIGEVI LNPYLGPRLK SGVVTTNMPM
DHDKPIDFGL QKFCESCNKC ARECPSGAIT AGPKLMFNGY EIWKSDSQKC TSYRITTLGG
SMCGRCMKTC PWNLEGLFAE APFRWAAMNL PGTAKALAKL DDKVGNGEIN AAKKWWWDLE
MIDEGPYDPS PHPVNARALS KDLDLKYEDQ TLAVYPAPLA PPPYNYPFPM DREAGITAYE
GMIDAKEHKR RRAAGDPPEH IYNPDQGESP VLQVVLSKVE TMTDLVTKYE FSMPDGSPMP
VVTAGAHVDV VVAPEFFRQY SLSGDPSNRN NYQIAVLRED EGRGGSKLMH RIFQEGRKLF
ISKPINHFPL VESASFTYLM GGGIGITPMI SMAHRLHSIG ADFAVHYSCS KRANAGFLND
LAKVPWADKV HYHFSDEDSR ANLHHVLKPH KDAHVYTCGP DTYMESVMSA AKHNGFPEDC
RHLEYFSVPE QPEYENFDFT FKLAKSGKVV HVPADTIPSD ALLAAGVSID VKCSDGLCGV
CKCNVVSGDV QHRDFVLSNK ERETQMIVCQ SRAAQKDGEV VLDI
//
