ID U5N9Y5_9BURK Unreviewed; 649 AA.
AC U5N9Y5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Heterodisulfide reductase subunit A {ECO:0000313|EMBL:AGX88217.1};
GN Name=hdrA {ECO:0000313|EMBL:AGX88217.1};
GN ORFNames=Cenrod_2147 {ECO:0000313|EMBL:AGX88217.1};
OS Candidatus Symbiobacter mobilis CR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX88217.1, ECO:0000313|Proteomes:UP000017184};
RN [1] {ECO:0000313|EMBL:AGX88217.1, ECO:0000313|Proteomes:UP000017184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:AGX88217.1};
RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA Overmann J., Bryant D.A.;
RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT phototrophic consortium "Chlorochromatium aggregatum".";
RL Genome Biol. 14:R127-R127(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the HdrA family.
CC {ECO:0000256|ARBA:ARBA00006561}.
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DR EMBL; CP004885; AGX88217.1; -; Genomic_DNA.
DR RefSeq; WP_022775388.1; NC_022576.1.
DR AlphaFoldDB; U5N9Y5; -.
DR STRING; 946483.Cenrod_2147; -.
DR KEGG; cbx:Cenrod_2147; -.
DR PATRIC; fig|946483.4.peg.2162; -.
DR eggNOG; COG1148; Bacteria.
DR HOGENOM; CLU_020302_0_0_4; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000017184; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR039650; HdrA-like.
DR PANTHER; PTHR43498:SF1; COB--COM HETERODISULFIDE REDUCTASE IRON-SULFUR SUBUNIT A; 1.
DR PANTHER; PTHR43498; FERREDOXIN:COB-COM HETERODISULFIDE REDUCTASE SUBUNIT A; 1.
DR Pfam; PF12831; FAD_oxidored; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 2.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 3.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000017184}.
FT DOMAIN 240..269
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 575..604
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 606..635
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 649 AA; 69050 MW; 362CBE93BAA3AE47 CRC64;
MNQPSRTAVI LCTCSGIITE RIDWDRVQQL LACHPTRPLF RIDDLACAAD HLEATAQWLR
EEQPDRLVVA ACSPREHEST FRKLMADAGL NPYFMQLVNV REQIAWVTAD PVQATAKAAR
MLSAALYRVQ RHVPLQERSF PVRSDVAVIG AGPAGIQAAL TLARAGRKVT LIEKEPFIGG
LPVRFEELFP NLDCGPCLLE PVMGEVLHGP ESESIQVLTL SEVTAVKGGF GNWNLTVRQS
PRYIDPELCI GCMECVAVCP ARRPNVWNGL SDMAAVGAPF AGALPNLPHI DPAACLRLND
SGGQDCDACV GQCPVEGALR FDDAPTTHSI DVGAIILATG CVEEDSLPGV FAGLADIHTA
YAFERLLAMN GPTEGELRTA RGGPPKSLAI VHCAGSLDED GVPYCSGTCC RDALKFAHLA
AHKVEGLSVT RLVREQMAPG VDAAHLFHHD QSRVVRYGGM DRLHVAGKGA DRVIVCTDTN
ERVAAEMIVL MRPLVPGQGT ASVCEVLELD RDGAGFIATA HSLAGSCSTA LKGVYLAGSC
RGPGDIREAF ATGTAAAGLV LSDLVAQRDI VVDPQVAVVD VDRCSGCVTC LPLCPYKAIS
WNDADRVAHI EDTLCQGCGT CVAACPAGAI EGRGFSRDML RAELEGILS
//