ID I1DVM9_9GAMM Unreviewed; 380 AA.
AC I1DVM9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN Name=yggW {ECO:0000313|EMBL:GAB58107.1};
GN ORFNames=RNAN_1078 {ECO:0000313|EMBL:GAB58107.1};
OS Rheinheimera nanhaiensis E407-8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=562729 {ECO:0000313|EMBL:GAB58107.1, ECO:0000313|Proteomes:UP000004374};
RN [1] {ECO:0000313|EMBL:GAB58107.1, ECO:0000313|Proteomes:UP000004374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E407-8 {ECO:0000313|EMBL:GAB58107.1,
RC ECO:0000313|Proteomes:UP000004374};
RX PubMed=23209246; DOI=10.1128/JB.01922-12;
RA Zhang X.-Y., Zhang Y.-J., Qin Q.-L., Xie B.-B., Chen X.-L., Zhou B.-C.,
RA Zhang Y.-Z.;
RT "Genome Sequence of the Protease-Producing Bacterium Rheinheimera
RT nanhaiensis E407-8T, Isolated from Deep-Sea Sediment of the South China
RT Sea.";
RL J. Bacteriol. 194:7001-7002(2012).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAB58107.1}.
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DR EMBL; BAFK01000004; GAB58107.1; -; Genomic_DNA.
DR RefSeq; WP_008219487.1; NZ_BAFK01000004.1.
DR AlphaFoldDB; I1DVM9; -.
DR STRING; 562729.RNAN_1078; -.
DR OrthoDB; 9808022at2; -.
DR Proteomes; UP000004374; 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; 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:UP000004374};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 2..238
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 380 AA; 42185 MW; F17003AA0B001445 CRC64;
MALQLPPLAL YIHIPWCIQK CPYCDFNSHA VKQGIPEQEY IAHVLADLDQ DLPLVKGRSI
SSIFIGGGTP SVFSASGIAQ ILTGVKQRIH CTDDMEVTME ANPGTVEADR FAGYVAGGVT
RFSIGVQSFQ TAQLKALGRI HDSAEAIRAA KLAQQLPLKS FNLDLMHGLP QQDIAGALAD
LQQAIGLNPP HLSWYQLTIE PNTAFASRPP VLPPDDTLWD IQQQGLALLQ QHGYQQYEIS
AYARAGQQCR HNLNYWRYGD YLGIGCGAHG KITLPSRNSI LRTVKIKHPK GYMDISRGYT
DSREQVEPDD RPFEFFMNRF RLLEPCPKAD FSAYTGLPLS HIDKAITEAA QKGLLTVSDS
HWQITDKGAR YLNDLLTLFI
//
