ID A0A1I2H1Z9_9GAMM Unreviewed; 387 AA.
AC A0A1I2H1Z9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN ORFNames=SAMN04488120_10181 {ECO:0000313|EMBL:SFF23420.1};
OS Fontimonas thermophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Fontimonas.
OX NCBI_TaxID=1076937 {ECO:0000313|EMBL:SFF23420.1, ECO:0000313|Proteomes:UP000199771};
RN [1] {ECO:0000313|EMBL:SFF23420.1, ECO:0000313|Proteomes:UP000199771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23609 {ECO:0000313|EMBL:SFF23420.1,
RC ECO:0000313|Proteomes:UP000199771};
RA de Groot N.N.;
RL Submitted (OCT-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; FOOC01000001; SFF23420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2H1Z9; -.
DR STRING; 1076937.SAMN04488120_10181; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000199771; 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; 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|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:UP000199771};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 2..242
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 387 AA; 42935 MW; CFF3E42CB04A258A CRC64;
MSLPTPPLAL YVHFPWCIRK CPYCDFNSHP LRGELPEHAY VNALLRDLDY ELQSVPIPAA
APPLVSIFMG GGTPSLFSAQ EIGSLLDGLS RRLAFAPDIE ITLEANPGTA EAQRFCGYRA
AGINRLSLGI QSLDDAQLRR LGRIHGSAEA VQAFQMARAA GFDNINLDLM YALPQQTPQD
AATDLRTLLA LAPEHVSYYQ LTLEPNTEFA LRPPPLPDED DAWAMHEQGL ALLDAAGYTQ
YEISAHARPG KPSRHNVNYW MFGDYLGIGA GAHGKRTLAD GRILRRARHK HPKTYLQHAG
TVAAIQEERT VAPTDLPFEF LMNALRLRDG FPIAEFTART GLAWDERIHG LREARARGLL
EETPERVRAS PLGWRHLNAV LRLFLDA
//
