ID Q5NRL8_ZYMMO Unreviewed; 393 AA.
AC Q5NRL8;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116};
GN OrderedLocusNames=ZMO0012 {ECO:0000313|EMBL:AAV88636.1};
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203 {ECO:0000313|EMBL:AAV88636.1, ECO:0000313|Proteomes:UP000001173};
RN [1] {ECO:0000313|EMBL:AAV88636.1, ECO:0000313|Proteomes:UP000001173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4 {ECO:0000313|Proteomes:UP000001173};
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.S., Chong H., Park H.S., Yoon K.O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.H., Kil J.I., Park C.J., Oh H.M., Lee J.S., Jin S.J.,
RA Um H.W., Lee H.J., Oh S.J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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 ---------------------------------------------------------------------------
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; AE008692; AAV88636.1; -; Genomic_DNA.
DR RefSeq; WP_011240000.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NRL8; -.
DR STRING; 264203.ZMO0012; -.
DR KEGG; zmo:ZMO0012; -.
DR eggNOG; COG0635; Bacteria.
DR HOGENOM; CLU_027579_0_1_5; -.
DR Proteomes; UP000001173; 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; 3.20.20.70; 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 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|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 Oxidoreductase {ECO:0000313|EMBL:AAV88636.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001173};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU364116}.
FT DOMAIN 13..248
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 393 AA; 43941 MW; C232335EA0860C02 CRC64;
MTEQALGKDK RQEKQDMPLA LYIHWPFCLA KCPYCDFNSH VRPDIDAALW QDALLSDMAH
EAALTQGRRL SSIFFGGGTP SLMSPETVAA LIDAATRYWQ PTSDIEITLE ANPSSVEADR
FQSLALAGVN RLSLGIQALD DTSLHFLGRI HNVQEALSAL DIAQKNFSRV SFDLIYGRPN
QSLKDWEEEL KQALAFGSDH LSLYQLTIEE GTRFHSLVRQ GQFTPMDGDK AADLFDLTRD
MTKAAGIPAY EISNHARKNS ESRHNLTYWR YGDYIGIGAG AHGRRLNNVT IRHKKPENWL
SAVQKQQQGI QEETPLSPKD QAIEAVLMGL RLTEGIHSEN IQKRTGLDIS EFLDLAAIQY
YSDQGLLTFN NGLLRITAQG VLLTDALIRE ISL
//