GenomeNet

Database: UniProt
Entry: A0A1B9ARF4_9BACI
LinkDB: A0A1B9ARF4_9BACI
Original site: A0A1B9ARF4_9BACI 
ID   A0A1B9ARF4_9BACI        Unreviewed;       376 AA.
AC   A0A1B9ARF4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN   ORFNames=A8L44_08610 {ECO:0000313|EMBL:OCA86456.1};
OS   Bacillus sp. FJAT-27986.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1743146 {ECO:0000313|EMBL:OCA86456.1, ECO:0000313|Proteomes:UP000092673};
RN   [1] {ECO:0000313|EMBL:OCA86456.1, ECO:0000313|Proteomes:UP000092673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-27986 {ECO:0000313|EMBL:OCA86456.1,
RC   ECO:0000313|Proteomes:UP000092673};
RA   Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Q., Zhu Y., Wang J.,
RA   Liu B., Liu G.;
RT   "Bacillus sp. FJAT-27986.";
RL   Submitted (MAY-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:OCA86456.1}.
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; MAYV01000014; OCA86456.1; -; Genomic_DNA.
DR   RefSeq; WP_066105276.1; NZ_MAYV01000014.1.
DR   AlphaFoldDB; A0A1B9ARF4; -.
DR   STRING; 1743146.A8L44_08610; -.
DR   OrthoDB; 9808022at2; -.
DR   Proteomes; UP000092673; 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   Reference proteome {ECO:0000313|Proteomes:UP000092673};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          1..232
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   376 AA;  43076 MW;  AE2DC2979016ED34 CRC64;
     MVKSLYIHIP FCTQICHYCD FNKFFIQNQP VDEYIQTLLT EMDLYNLSQN EPLSTVFIGG
     GTPSALEPLQ LEQLLFSMKE KVTLAPGYEY TVEANPGDLS KDKLRIMKEA GVNRLSLGVQ
     SFNEELLKKI GRAHNVKDVY ETIDMAREEG FDNISIDLIY SLPGQTLSDL EDTVDRALQL
     NLPHFSAYSL IIEPKTVFYI MLNKGKLSLP GEDAEATMYE YVMERLVEVG YNQYEISNFA
     KKGFESRHNL VYWNNEEYYG LGAGAHGYLD AVRYHNHGPL KKYMNAIQDG RKPIVEQATV
     TRKEQMEEEM FLGLRKMEGV SLEHFQKRFS VNINDVFGET IKRMVSEGLL ELVNGRVRLT
     HPGKLMGNEV FQAFLL
//
DBGET integrated database retrieval system