ID A0A1A8XWA7_9RHOO Unreviewed; 419 AA.
AC A0A1A8XWA7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN Name=yggW {ECO:0000313|EMBL:SBT09294.1};
GN ORFNames=PROAA_320004 {ECO:0000313|EMBL:SBT09294.1};
OS Candidatus Propionivibrio aalborgensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Propionivibrio.
OX NCBI_TaxID=1860101 {ECO:0000313|EMBL:SBT09294.1, ECO:0000313|Proteomes:UP000199600};
RN [1] {ECO:0000313|EMBL:SBT09294.1, ECO:0000313|Proteomes:UP000199600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2 {ECO:0000313|EMBL:SBT09294.1};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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}.
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DR EMBL; FLQY01000246; SBT09294.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A8XWA7; -.
DR Proteomes; UP000199600; 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|RuleBase:RU364116};
KW Reference proteome {ECO:0000313|Proteomes:UP000199600};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 28..265
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 419 AA; 46112 MW; EE6D1EB2AA0463FE CRC64;
MSARNAARVI PIVPLSKAQS QAGGKLEFRS PPPLSLYVHI PWCVRKCPYC DFNSHEVRGQ
KAGEVIPEAA YIGALIADLE SALPLVWGRK VSSIFFGGGT PSLLSGQALD ELLTAIRTLL
PVVPDAEVTL EANPGTVEAE KFAAFREAGI NRLSLGIQSF NPSHLKALGR IHSDSDARRA
IEIAASHFDN FNLDLMYGLP GQTLEQALAD VDNALAFSPP HLSCYQLTIE PNTAFAAAPP
ILPDSDRCAD MQDAIEAKLA GAVGSAGFTH YETSAFARPG RQCRHNLNYW HFGDYLGIGA
GAHGKLTLHD RVLRQMRWKQ PKQYMAKVAE GAPVQEEFSV ETTGLTFEFM MNALRLNRGF
DARLFELRTS LPLITIESEL RRAVDEGLIE RKPGHIAPTD RGRRYLNRLL EMFLVERPT
//
