ID A0A1B2AFE6_9SPHN Unreviewed; 381 AA.
AC A0A1B2AFE6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN Name=hemN_2 {ECO:0000313|EMBL:ANY20873.1};
GN ORFNames=A6F68_02374 {ECO:0000313|EMBL:ANY20873.1};
OS Tsuneonella dongtanensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Tsuneonella.
OX NCBI_TaxID=692370 {ECO:0000313|EMBL:ANY20873.1, ECO:0000313|Proteomes:UP000092932};
RN [1] {ECO:0000313|EMBL:ANY20873.1, ECO:0000313|Proteomes:UP000092932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22672 {ECO:0000313|EMBL:ANY20873.1,
RC ECO:0000313|Proteomes:UP000092932};
RA Cheng H., Wu Y.-H., Zhou P., Huo Y.-Y., Wang C.-S., Xu X.-W.;
RT "Complete genome sequence of Altererythrobacter dongtanensis KCTC 22672, a
RT type strain with esterase isolated from tidal flat.";
RL Submitted (JUL-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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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}.
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DR EMBL; CP016591; ANY20873.1; -; Genomic_DNA.
DR RefSeq; WP_067680289.1; NZ_CP016591.1.
DR AlphaFoldDB; A0A1B2AFE6; -.
DR STRING; 692370.A6F68_02374; -.
DR KEGG; ado:A6F68_02374; -.
DR PATRIC; fig|692370.5.peg.2388; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000092932; Chromosome.
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; 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 Oxidoreductase {ECO:0000313|EMBL:ANY20873.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092932};
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 381 AA; 41526 MW; B23FD34CB2DC2CDA CRC64;
MARALYIHWP FCLKKCPYCD FNSHVRDAVE VDAWQTGLLA DMRHEAALAG GEPLESIFFG
GGTPSLMPPA LVGALLDEAE RLWGFAPDIE ITLEANPSSV EAAAFAGLAA AGVNRVSLGI
QSLDDAALRF LGRLHDANEG LRALDTAQHV FRRVNADFIY ARPGQSAEAW SEELQRALAL
GTDHLSLYQL TIEPGTRFAT DVRLGAFAPL DDDPAADLFA LTRAMTDEAG LPAYEVSNHA
RPGHESRHNL TYWRYRDYVG IGPGAHGRRG GVATVRHKKP ENWLDAVIRA DHGIAEERQL
GLREQASEAL LMGLRLAEGV DLAAMRARFG IEELLDPDRL AFHRDLGFVE ISGERIRVTE
AGMPLLDALL GELVPAALVE A
//
