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Database: UniProt
Entry: D4H369_DENA2
LinkDB: D4H369_DENA2
Original site: D4H369_DENA2 
ID   D4H369_DENA2            Unreviewed;       363 AA.
AC   D4H369;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN   OrderedLocusNames=Dacet_0353 {ECO:0000313|EMBL:ADD67153.1};
OS   Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Geovibrionaceae; Denitrovibrio.
OX   NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD67153.1, ECO:0000313|Proteomes:UP000002012};
RN   [1] {ECO:0000313|EMBL:ADD67153.1, ECO:0000313|Proteomes:UP000002012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12809 / NBRC 114555 / N2460
RC   {ECO:0000313|Proteomes:UP000002012};
RX   PubMed=21304711; DOI=10.4056/sigs.892105;
RA   Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA   Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT   (N2460).";
RL   Stand. Genomic Sci. 2:270-279(2010).
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; CP001968; ADD67153.1; -; Genomic_DNA.
DR   RefSeq; WP_013009698.1; NC_013943.1.
DR   AlphaFoldDB; D4H369; -.
DR   STRING; 522772.Dacet_0353; -.
DR   PaxDb; 522772-Dacet_0353; -.
DR   KEGG; dap:Dacet_0353; -.
DR   eggNOG; COG0635; Bacteria.
DR   HOGENOM; CLU_027579_2_2_0; -.
DR   InParanoid; D4H369; -.
DR   OrthoDB; 9808022at2; -.
DR   Proteomes; UP000002012; 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   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; SFLDG01065; anaerobic_coproporphyrinogen-I; 1.
DR   SFLD; SFLDF00562; HemN-like__clustered_with_heat; 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:ADD67153.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002012};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          1..224
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   363 AA;  41474 MW;  98AA1E371E1D5539 CRC64;
     MKGLYVHLPF CRNKCAYCGF YSETDCYDTQ ADYFKALISD LRSRKKHAYE TLYIGGGTPS
     TADRKLLASF LDAVSITCRW DFKESTIEAN PESIDKEFCR IVDFYKFSRV SIGCQSTSDD
     VLQKLTRIHS ASDIFHSYDM VRKLCPDTDV SLDMMYDIPG TQFESTYKTL KDLIALNPEH
     ISAYTYSFDT EFLKEGDADA TDFMVVRDEL ENAGYVKYEI SNFARPGHES MHNINYWMLG
     EYDGIGSSAW SLSYEDGKRI LRGKSDNLPE YIHSPKEYAE TEITEPPQTA LEEIVFGLRL
     AKGLDAEKIC TNVNAELKEK IYNLFSDLSE KELLSWDGSN VSLKKRGELL LDSVQSLLWQ
     LLP
//
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