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Database: UniProt
Entry: K9GWK6_9PROT
LinkDB: K9GWK6_9PROT
Original site: K9GWK6_9PROT 
ID   K9GWK6_9PROT            Unreviewed;       406 AA.
AC   K9GWK6;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN   ORFNames=C882_4349 {ECO:0000313|EMBL:EKV30390.1};
OS   Caenispirillum salinarum AK4.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Novispirillaceae; Caenispirillum.
OX   NCBI_TaxID=1238182 {ECO:0000313|EMBL:EKV30390.1, ECO:0000313|Proteomes:UP000009881};
RN   [1] {ECO:0000313|EMBL:EKV30390.1, ECO:0000313|Proteomes:UP000009881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK4 {ECO:0000313|EMBL:EKV30390.1,
RC   ECO:0000313|Proteomes:UP000009881};
RX   PubMed=23409257;
RA   Khatri I., Singh A., Korpole S., Pinnaka A.K., Subramanian S.;
RT   "Draft Genome Sequence of an Alphaproteobacterium, Caenispirillum salinarum
RT   AK4(T), Isolated from a Solar Saltern.";
RL   Genome Announc. 1:E00199-12(2013).
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}.
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:EKV30390.1}.
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DR   EMBL; ANHY01000008; EKV30390.1; -; Genomic_DNA.
DR   RefSeq; WP_009540457.1; NZ_ANHY01000008.1.
DR   AlphaFoldDB; K9GWK6; -.
DR   STRING; 1238182.C882_4349; -.
DR   PATRIC; fig|1238182.3.peg.2011; -.
DR   eggNOG; COG0635; Bacteria.
DR   Proteomes; UP000009881; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000009881};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU364116}.
FT   DOMAIN          5..244
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   406 AA;  44625 MW;  AA2DA13A541F5AC8 CRC64;
     MTDHIQGDEG FGLYVHWPFC LSKCPYCDFN SHVVDRVDHG RFRAALRVEL AHYAAMAGRE
     GRRLTSVFFG GGTPSLMEPG TVAAILEDAR SLFTPANDLE VTLEANPGAV DRAKFEDFRD
     AGVNRVSLGV QALDDAALAF LGRRHDRAEA LAALEAAQSL FPRTSIDLIY ARPGHDPEAW
     RQELRQALDI LAGHGHLSLY QLTVEQGTKF YLDWHRGDWR LPEEDDAVSL WHVTQEETAR
     AGLPSYEVSN HARPGEECRH NLVYWRGGDY IGVGPGAHGR LTVGGTPRAT RQHRAPERWL
     SQVEAHGHAT TRDDPLGQAE RAEELLLMGL RLTEGVDKMR FHRLSGRPLD GFVDARALAD
     LTEMGLLEDT PAALRATADG MLVLNGLIAA LVPVDGDAED GSPPGR
//
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