ID B3QWC9_CHLT3 Unreviewed; 376 AA.
AC B3QWC9;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN OrderedLocusNames=Ctha_0774 {ECO:0000313|EMBL:ACF13242.1};
OS Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chloroherpetonaceae;
OC Chloroherpeton.
OX NCBI_TaxID=517418 {ECO:0000313|EMBL:ACF13242.1, ECO:0000313|Proteomes:UP000001208};
RN [1] {ECO:0000313|EMBL:ACF13242.1, ECO:0000313|Proteomes:UP000001208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35110 / GB-78 {ECO:0000313|Proteomes:UP000001208};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
RL Submitted (JUN-2008) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001100; ACF13242.1; -; Genomic_DNA.
DR AlphaFoldDB; B3QWC9; -.
DR STRING; 517418.Ctha_0774; -.
DR KEGG; cts:Ctha_0774; -.
DR eggNOG; COG0635; Bacteria.
DR HOGENOM; CLU_027579_0_1_10; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000001208; 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; 3.80.30.20; tm_1862 like domain; 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 InterPro; IPR023404; rSAM_horseshoe.
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; 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 Oxidoreductase {ECO:0000313|EMBL:ACF13242.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001208};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 1..230
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 376 AA; 42878 MW; 3B0D41A6E0860995 CRC64;
MPGLYFHIPF CRRRCHYCDF YFTTNASLIG RFLVGLEAEI FHKATLFENE TIETIYFGGG
TPSLLSLAQI ERVLALCFAH FRIAPAPEIT LEANPEDLNE EKLQALASSP VNRLSLGIQS
FDAGKLKRLS RGHSAQESFE IASLARTFFR NINIDLMFGT PDESLNDWQR ELETALQFQP
EHLSTYSLTV EPKTLLAHDI GLGKIPAPNE SLQVEMFLSV MRRLREAGYR HYEVSNFAKP
AALSAHNFDA WQRKPYLGFG PAAHSFVRQG RTERRFANVR NLKTYLENPA NALLFEETLT
EKDILNEEIF LALRQDTGLG MDVLEKRRKF TRSNLLEKEI EAFCLQGLLR RDSGRLRLTD
KGFTLADSIA ETFMVE
//