ID A0A0A5GCS3_9BACI Unreviewed; 381 AA.
AC A0A0A5GCS3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=N784_00925 {ECO:0000313|EMBL:KGX88930.1};
OS Pontibacillus litoralis JSM 072002.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385512 {ECO:0000313|EMBL:KGX88930.1, ECO:0000313|Proteomes:UP000030401};
RN [1] {ECO:0000313|EMBL:KGX88930.1, ECO:0000313|Proteomes:UP000030401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSM 072002 {ECO:0000313|EMBL:KGX88930.1,
RC ECO:0000313|Proteomes:UP000030401};
RA Huang J., Wang G.;
RL Submitted (AUG-2013) 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:KGX88930.1}.
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DR EMBL; AVPG01000001; KGX88930.1; -; Genomic_DNA.
DR RefSeq; WP_036831035.1; NZ_AVPG01000001.1.
DR AlphaFoldDB; A0A0A5GCS3; -.
DR STRING; 1385512.N784_00925; -.
DR eggNOG; COG0635; Bacteria.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000030401; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364116};
KW Reference proteome {ECO:0000313|Proteomes:UP000030401};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..229
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 381 AA; 44753 MW; 0FB0A478A15A9DF9 CRC64;
MITSAYIHIP FCQQICHYCD FTKFFYNEDL ANQYLEALDK EIETAVGKKQ TYMRTIFVGG
GTPTALNYHQ LEKLLQTIAS AFDVNNCEEY TFEANPGEFD EQKLTLLKRY GVNRISFGVQ
VFDDQMLKKI GRLHRVQDVY DNLRLFEKHQ FDNVSIDLIY GLPDQTLEHF QHTLDEAIQL
DLPHYSTYCL QIEPKTVFYQ RYQKGKLHKP VEELEADMYD MLVHKMEGNG NVQYEISNFA
RPGFESKHNL TYWNNEYYYG FGAGSHGYVP GYRTVNIRPL PRYIEQAKET GMPILHKEEV
TLQAQIEEQM FLGLRKKEGV SKSQFFNRFG RPIETLYEQP LTYLQEKGWM EEEGDYVRVT
SNGRLFANSV FQEFLLESIE E
//
