GenomeNet

Database: UniProt
Entry: A0A0B0HBQ6_SOVGS
LinkDB: A0A0B0HBQ6_SOVGS
Original site: A0A0B0HBQ6_SOVGS 
ID   A0A0B0HBQ6_SOVGS        Unreviewed;       385 AA.
AC   A0A0B0HBQ6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN   ORFNames=JV46_17190 {ECO:0000313|EMBL:KHF26485.1};
OS   Solemya velum gill symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=2340 {ECO:0000313|EMBL:KHF26485.1, ECO:0000313|Proteomes:UP000030856};
RN   [1] {ECO:0000313|EMBL:KHF26485.1, ECO:0000313|Proteomes:UP000030856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH {ECO:0000313|EMBL:KHF26485.1,
RC   ECO:0000313|Proteomes:UP000030856};
RX   PubMed=25342549; DOI=10.1186/1471-2164-15-924;
RA   Dmytrenko O., Russell S.L., Loo W.T., Fontanez K.M., Liao L., Roeselers G.,
RA   Sharma R., Stewart F.J., Newton I.L., Woyke T., Wu D., Lang J.M.,
RA   Eisen J.A., Cavanaugh C.M.;
RT   "The genome of the intracellular bacterium of the coastal bivalve, Solemya
RT   velum: a blueprint for thriving in and out of symbiosis.";
RL   BMC Genomics 15:924-924(2014).
CC   -!- FUNCTION: Probably acts as a heme chaperone, transferring heme to an
CC       unknown acceptor. Binds one molecule of heme per monomer, possibly
CC       covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|RuleBase:RU364116}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364116}.
CC   -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC       family. HemW subfamily. {ECO:0000256|ARBA:ARBA00006100}.
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:KHF26485.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JRAA01000001; KHF26485.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B0HBQ6; -.
DR   STRING; 2340.JV46_17190; -.
DR   PATRIC; fig|2340.3.peg.998; -.
DR   eggNOG; COG0635; Bacteria.
DR   OMA; HIPWCVR; -.
DR   OrthoDB; 9808022at2; -.
DR   Proteomes; UP000030856; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR010723; HemN_C.
DR   InterPro; IPR004559; HemW-like.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR00539; hemN_rel; 1.
DR   PANTHER; PTHR13932; COPROPORPHYRINIGEN III OXIDASE; 1.
DR   PANTHER; PTHR13932:SF5; HEME CHAPERONE-RELATED; 1.
DR   Pfam; PF06969; HemN_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR   SFLD; SFLDF00562; HemN-like__clustered_with_heat; 1.
DR   SFLD; SFLDF00288; HemN-like__clustered_with_nucl; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU364116};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU364116};
KW   Cytoplasm {ECO:0000256|RuleBase:RU364116};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU364116};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364116};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364116};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364116};
KW   Oxidoreductase {ECO:0000313|EMBL:KHF26485.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030856};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          5..239
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   385 AA;  42452 MW;  814FFFBAEDA735F9 CRC64;
     MAMLQADSIP LSLYIHMPWC ERKCPYCDFN SHASSNIEEE SYIDALLQDF EGELELPGVR
     ARKINSVFIG GGTPSLFSAV AIKRLLSGIA QRAACEETEI TLEANPGSAD SSKFAGYREA
     GVNRLSIGIQ SFDDEKLAAL GRIHNRETAI HAIEKARAAG FDNLNLDLMF GLPAQSEGEA
     MLDLQQATSF QPEHLSWYQL TLEPNTPFNH SPPAALADND QLADFSTKGI GQLQQAGFSQ
     YEVSAYAQPG KACRHNLNYW QFGDYLGIGA GAHAKITLAD GTIVRRSKQR HPQRYLAAAT
     ATDAVSSSRA LTDDDLPLEY MMNALRLNEG FRQQDFELRT GLAFSSIEET LGEQVKKGLL
     ERDGDSWRTS EIGRLHLDNL LLEFS
//
DBGET integrated database retrieval system