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Database: UniProt
Entry: W3Y5T7_9FIRM
LinkDB: W3Y5T7_9FIRM
Original site: W3Y5T7_9FIRM 
ID   W3Y5T7_9FIRM            Unreviewed;       395 AA.
AC   W3Y5T7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN   ORFNames=HMPREF1521_0261 {ECO:0000313|EMBL:ETS93553.1};
OS   Veillonella sp. AS16.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=936589 {ECO:0000313|EMBL:ETS93553.1, ECO:0000313|Proteomes:UP000019042};
RN   [1] {ECO:0000313|EMBL:ETS93553.1, ECO:0000313|Proteomes:UP000019042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS16 {ECO:0000313|EMBL:ETS93553.1,
RC   ECO:0000313|Proteomes:UP000019042};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JAN-2014) 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:ETS93553.1}.
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DR   EMBL; AZYX01000007; ETS93553.1; -; Genomic_DNA.
DR   AlphaFoldDB; W3Y5T7; -.
DR   PATRIC; fig|936589.3.peg.277; -.
DR   eggNOG; COG0635; Bacteria.
DR   Proteomes; UP000019042; 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; 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|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   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          11..250
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   395 AA;  45455 MW;  CEA239A4744D6B75 CRC64;
     MIQTDSKTMN LFTIGDMGLY VHIPFCKQKC IYCDFPAYQN LQDYYETYIY ALVQEIDLWA
     NEHPESKLRP IDTIYFGGGT PTELSIDQLK MILDKIRHTF TIIDSCHMTI ESNPGEVVLI
     YLIKLVSLGF NRISFGIQTF DDKALSRLHR SHTAKKAIQA VQDAKKAGFE DINIDLIYGL
     PNQTVADVQR NLELVRDLPI NHISTYGLQV EAGTYLYHLV KKKLISLPDE SIDESMYDTM
     MTGLCELGFE RYEISNFAKG GSYSRHNLKY WHYIDYLGFG AGAHSFYDGV RRSNNRNVMP
     YIQSVDRYEM PTVETENISI ERAQEDFCFL ALRTKWGLDE KLFKDRFGIS VRNLFGPSID
     ELVAKGLMNF HHGAYHVTPE GAKHGNYVFG QFIRE
//
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