ID A0A0N0XJC6_9NEIS Unreviewed; 397 AA.
AC A0A0N0XJC6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|RuleBase:RU364116};
GN Name=hemN_2 {ECO:0000313|EMBL:KPC53697.1};
GN ORFNames=WG78_07635 {ECO:0000313|EMBL:KPC53697.1};
OS Amantichitinum ursilacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Amantichitinum.
OX NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC53697.1, ECO:0000313|Proteomes:UP000037939};
RN [1] {ECO:0000313|EMBL:KPC53697.1, ECO:0000313|Proteomes:UP000037939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGB-41 {ECO:0000313|EMBL:KPC53697.1,
RC ECO:0000313|Proteomes:UP000037939};
RA Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT chitin-degrading bacterium.";
RL Submitted (JUL-2015) 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 -!- 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:KPC53697.1}.
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DR EMBL; LAQT01000005; KPC53697.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0XJC6; -.
DR STRING; 857265.WG78_07635; -.
DR PATRIC; fig|857265.3.peg.1563; -.
DR Proteomes; UP000037939; 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; SFLDG01082; B12-binding_domain_containing; 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 Oxidoreductase {ECO:0000313|EMBL:KPC53697.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037939};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 15..247
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 397 AA; 44572 MW; 2B27FE7CC90900F4 CRC64;
MQSISMPVSS STWQMTALPP LALYIHFPWC VKKCPYCDFN SHTLREGVPE AQYIDALLRD
LETCLPLTWG RQVSTIFMGG GTPSLFSAEA MEQLLAGIRA RVRLQPDAEI TMEANPGTFE
ADKFAGYRAA GINRLSIGIQ SFNAGHLQAL GRIHNDDEAH KAIEIAKRHF DNFNLDIMYA
LPQQTLAQAL SDIDTAIAAG PTHLSAYHLT LEPNTLFHRY PPALPDDDTA ADMQEAIEQH
LASAGFEHYE TSAFCRPGRQ AKHNLNYWKF GDYIGIGAGA HGKISFHDRI IRQMRYKQPG
EYLAQMAAGN AVQTEEPVTL EQLPFEFMLN ALRLVDGFDL DLFTQRTGLP LTRVIHEIER
ATADGLLERD PNDLHRIRPT LRGQRFLNTL LERFLPD
//
