HEMW_SYNY3
ID HEMW_SYNY3 Reviewed; 412 AA.
AC P73245;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Heme chaperone HemW;
DE AltName: Full=Oxygen-independent coproporphyrinogen-III oxidase-like protein sll1917;
GN Name=hemW {ECO:0000250|UniProtKB:P52062}; OrderedLocusNames=sll1917;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, FE-S CLUSTER-BINDING, AND INDUCTION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=20194361; DOI=10.1093/pcp/pcq023;
RA Goto T., Aoki R., Minamizaki K., Fujita Y.;
RT "Functional differentiation of two analogous coproporphyrinogen III
RT oxidases for heme and chlorophyll biosynthesis pathways in the
RT cyanobacterium Synechocystis sp. PCC 6803.";
RL Plant Cell Physiol. 51:650-663(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 (By similarity). Binds 1 [2Fe-2S] cluster. Although this
CC protein has sequence motifs typically found in proteins binding the
CC [4Fe-4S]-AdoMet radical-SAM cluster and S-adenosylmethionine,
CC spectroscopic evidence suggests that a [2Fe-2S] cluster is present; S-
CC adenosylmethionine was not detected. Has no detectable
CC coproporphyrinogen-III oxidase activity (PubMed:20194361).
CC {ECO:0000250|UniProtKB:P32131, ECO:0000269|PubMed:20194361}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01266};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9CGF7}.
CC -!- INDUCTION: Induced under microoxic conditions.
CC {ECO:0000269|PubMed:20194361}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have no detectable
CC phenotype. {ECO:0000269|PubMed:20194361}.
CC -!- MISCELLANEOUS: Might carry two S-adenosyl-L-methionine binding sites
CC with only one binding to the iron-sulfur cluster.
CC {ECO:0000250|UniProtKB:P32131}.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. HemW subfamily. {ECO:0000305}.
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DR EMBL; BA000022; BAA17272.1; -; Genomic_DNA.
DR PIR; S75358; S75358.
DR AlphaFoldDB; P73245; -.
DR SMR; P73245; -.
DR IntAct; P73245; 1.
DR STRING; 1148.1652349; -.
DR PaxDb; P73245; -.
DR PRIDE; P73245; -.
DR EnsemblBacteria; BAA17272; BAA17272; BAA17272.
DR KEGG; syn:sll1917; -.
DR eggNOG; COG0635; Bacteria.
DR InParanoid; P73245; -.
DR OMA; HIPWCVR; -.
DR PhylomeDB; P73245; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.80.30.20; -; 1.
DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR004559; HemW-like.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR PANTHER; PTHR13932; PTHR13932; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00562; HemN-like__clustered_with_heat; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00539; hemN_rel; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Chaperone; Cytoplasm; Heme; Iron; Iron-sulfur; Metal-binding;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..412
FT /note="Heme chaperone HemW"
FT /id="PRO_0000109961"
FT DOMAIN 4..241
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 13
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 19
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305|PubMed:20194361"
FT BINDING 23
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305|PubMed:20194361"
FT BINDING 26
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000305|PubMed:20194361"
FT BINDING 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 73..74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 169
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
SQ SEQUENCE 412 AA; 46447 MW; D394AC03CE1B8D3D CRC64;
MNTGTYLMPT AAYIHIPFCR QRCFYCDFPI AVTGFQSLTL DGWVGEYVEA VCREIAGQQH
QGQPLQTVFF GGGTPSLLPI TGLEKILLAV DQYLGIAPDA EISIEIDPGT FDQVQLQGYK
NLGINRFSLG VQAFQDNLLA LCGRHHRRRD IDQALTAIAK ENIENWSLDL ITGLPEQTAA
DWHSSLTLAL AAGPKHISCY DLVLEPQTVF DKWEQRGKLA VPPPERSADF YRHGQEVLTQ
AGFHHYEISN YGRPGHQCRH NQIYWRNLPY YGLGMGATSY IDGKRFGRPR TRNGYYQWLE
SWLNQGCPIP GERVSPLENL LESLMLGLRL TAGVTWAQLP SVNQTEKAKI LATLTSFGDR
RWLEFYGEDN QMLAPNQTTT ETVQRFCFTD PEGILYSNQI LSALFAALEE DF
