ID A0A425W2L0_9FIRM Unreviewed; 388 AA.
AC A0A425W2L0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=DUD26_07985 {ECO:0000313|EMBL:RRF91990.1};
OS Eubacteriaceae bacterium.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae.
OX NCBI_TaxID=2049045 {ECO:0000313|EMBL:RRF91990.1, ECO:0000313|Proteomes:UP000285774};
RN [1] {ECO:0000313|EMBL:RRF91990.1, ECO:0000313|Proteomes:UP000285774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EUB1 {ECO:0000313|EMBL:RRF91990.1};
RA Scarborough M.J., Lawson C.E., Hamilton J., Donohue T.J., Noguera D.R.;
RT "Metatranscriptomic and thermodynamic insights into medium-chain fatty acid
RT production using an anaerobic microbiome.";
RL Submitted (JUL-2018) 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:RRF91990.1}.
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DR EMBL; QOUT01000011; RRF91990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A425W2L0; -.
DR Proteomes; UP000285774; 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; 3.30.750.200; -; 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 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; 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|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:UP000285774};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..239
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 388 AA; 44037 MW; DFB7953124569777 CRC64;
MDHALEIYIH IPFCRSKCRY CDFVSWPEHD LNRVKQYFEA LKREIAAFPY SGALPIRSVY
FGGGTPSAVP SSLLSDTIGA LEEKFGFDFQ RAAFEKTIEV NPKTVDEKKL YYYRRLGFNR
LSVGVQSFND ELLKTIGRLH TADEAEKTLR DAAAAGYDNI SADLIFGLPG QTLEDVDQTI
DKLSHFAPVR HISCYSLIVE PGTVFEKWQR EGRLALPDER TERAMYHDIC ERLAENGFEQ
YEISNFARPG YLSRHNSGYW DLTPYAGFGL GAASLFLENK APGEDGAFLR KTTTADFDTY
LQNPAACDEK HRLSKKEAEG DYMFLGLRRT KGVDDRDFQT LFGESIENRY AGEIHSLIEE
GLLEREGSRI RLTTLGLDLA NQVFMAFV
//
