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Database: UniProt
Entry: R5J7E6_9BACE
LinkDB: R5J7E6_9BACE
Original site: R5J7E6_9BACE 
ID   R5J7E6_9BACE            Unreviewed;       377 AA.
AC   R5J7E6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN   ORFNames=BN523_02519 {ECO:0000313|EMBL:CCY50493.1};
OS   Bacteroides sp. CAG:189.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1262737 {ECO:0000313|EMBL:CCY50493.1, ECO:0000313|Proteomes:UP000018406};
RN   [1] {ECO:0000313|EMBL:CCY50493.1, ECO:0000313|Proteomes:UP000018406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:189 {ECO:0000313|Proteomes:UP000018406};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:CCY50493.1}.
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DR   EMBL; CAYI010000117; CCY50493.1; -; Genomic_DNA.
DR   RefSeq; WP_005933578.1; NZ_HF991091.1.
DR   AlphaFoldDB; R5J7E6; -.
DR   GeneID; 77203520; -.
DR   Proteomes; UP000018406; 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; 3.80.30.20; tm_1862 like domain; 1.
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   InterPro; IPR023404; rSAM_horseshoe.
DR   NCBIfam; TIGR00539; hemN_rel; 1.
DR   PANTHER; PTHR13932; COPROPORPHYRINIGEN III OXIDASE; 1.
DR   PANTHER; PTHR13932:SF5; RADICAL S-ADENOSYL METHIONINE DOMAIN-CONTAINING PROTEIN 1, MITOCHONDRIAL; 1.
DR   Pfam; PF06969; HemN_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01065; anaerobic_coproporphyrinogen-I; 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   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|RuleBase:RU364116};
KW   Cytoplasm {ECO:0000256|RuleBase:RU364116};
KW   Heme {ECO:0000256|RuleBase:RU364116}; Iron {ECO:0000256|RuleBase:RU364116};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU364116};
KW   Metal-binding {ECO:0000256|RuleBase:RU364116};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018406};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          1..231
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   377 AA;  43481 MW;  885FFD93F75517E0 CRC64;
     MAGIYIHIPF CKTRCIYCDF YSTTLSEFKG RYIQTLCREL EIRRDYLQGA PIETIYLGGG
     TPSQLTQEDF LQIFETIERV YGMKQVREIT LEANPDDLTP EYTRMLATLP FNRISMGIQT
     FNEKTLQLLK RRHTAPQAIA AVEHCRKAGF QNISIDLIYG LPGETAESWK YDLKQAIALN
     VEHISAYHLI YEEGTPMYNM LQQHRISEVD EESSVGFFSE LIDQLTTAGY EHYEISNFSR
     PGYHSQHNTA YWKNIPYLGC GPSAHSFNRQ EREWNIASLN DYINGIENGK RIYETEDLNT
     VTRYNEFIIT SLRTCWGIPL AKLKEEFGTG LWQYCLDSAA LSLKNGKLIE KDNALRLTRE
     GIFISDSIMS DLLKIEE
//
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