ID A0A3P5X1U1_9RHOB Unreviewed; 390 AA.
AC A0A3P5X1U1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN Name=hemN_1 {ECO:0000313|EMBL:VDC21899.1};
GN ORFNames=XINFAN_00665 {ECO:0000313|EMBL:VDC21899.1};
OS Pseudogemmobacter humi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudogemmobacter.
OX NCBI_TaxID=2483812 {ECO:0000313|EMBL:VDC21899.1, ECO:0000313|Proteomes:UP000277498};
RN [1] {ECO:0000313|EMBL:VDC21899.1, ECO:0000313|Proteomes:UP000277498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACIP111625 {ECO:0000313|EMBL:VDC21899.1};
RA Criscuolo A.;
RL Submitted (NOV-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 -!- 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; UXAW01000036; VDC21899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P5X1U1; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000277498; 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; 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 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 Oxidoreductase {ECO:0000313|EMBL:VDC21899.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000277498};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 11..247
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 390 AA; 43567 MW; D7B657E331EB7DB2 CRC64;
MFHVKHSAPE DWQEGGFALY IHWPFCKAKC PYCDFNSHVR QRIDQDEWRR AYLAELDRAA
AETGGRILRS VFFGGGTPSL MDPAVTGAIL DRIARHWRLA NDLEVTLEAN PTSVEAARFT
GYRQAGVNRV SLGLQALNDL DLRRLGRQHS AAEGLAALDL ARSIFERTSC DLIYARQDQD
LPAWEEELRS VLTRGPDHIS LYQLTIEEGT AFARLFDAGK LAGLPDEDLA ADMYELTAGI
CAEYGLHDYE VSNYAREGAE SRHNLVYWRM GDYLGIGPGA HGRLTLDGIR YATSTHRSPE
LWLEAVRQGK GELPREVIPR ASQAVEYMMM SMRLTEGMSL ARYTALNGAP PKAMRELTES
GMIRIENDRL AATPAGRLLL NRLVLELSGA
//