ID A0A2N8NA67_9BACT Unreviewed; 377 AA.
AC A0A2N8NA67;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=BHU16_00590 {ECO:0000313|EMBL:PNE25648.1};
OS Tannerella sp. oral taxon 808.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Tannerella.
OX NCBI_TaxID=712711 {ECO:0000313|EMBL:PNE25648.1, ECO:0000313|Proteomes:UP000235918};
RN [1] {ECO:0000313|EMBL:PNE25648.1, ECO:0000313|Proteomes:UP000235918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cell103 {ECO:0000313|EMBL:PNE25648.1};
RA Beall C.J., Campbell A.G., Griffen A.L., Podar M., Leys E.J.;
RT "Genomics of the uncultivated, periodontitis-associated bacterium
RT Tannerella sp. BU045 (oral taxon 808).";
RL Submitted (SEP-2016) 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:PNE25648.1}.
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DR EMBL; MIQB01000002; PNE25648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N8NA67; -.
DR Proteomes; UP000235918; 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; 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; 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:UP000235918};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..232
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 377 AA; 42619 MW; 9EF856C5A4822965 CRC64;
MAGIYIHVPF CTQRCIYCDF YSQTDMARQA DYLRAVRREL EMRADELDGE PVETIYFGGG
TPSQLRGEDL GAIVRTIGRH YSLANHCEVT LEANPDDLTD AYLRDLFANV IIDRISLGVQ
SFSDADLRFL NRRHDAAGAI EAVRRLQDAG VKDISIDLIY GLPGQTPEAW VRNLDVAFGL
GVTHLSAYHL TYEAGTRLGR MLQRGDVCPV DEDTSVSLYS LLTERAAAAG FVHYEVSNFC
RPGWFARHNT AYWTGAKYLG IGPSAHSYDG QSRRWNVASL GRYIEGMEIR QPQYEREVLD
GDMRYNEYIM TRLRTMWGVR LSVIREVWGE CRVAHFLRQA APFLAAGRLV RLSENDTVRL
TEAAFFVSDG IISELFV
//
