CTAA_EXIS2
ID CTAA_EXIS2 Reviewed; 297 AA.
AC B1YIW6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Heme A synthase {ECO:0000255|HAMAP-Rule:MF_01664};
DE Short=HAS {ECO:0000255|HAMAP-Rule:MF_01664};
DE EC=1.17.99.9 {ECO:0000255|HAMAP-Rule:MF_01664};
DE AltName: Full=Cytochrome aa3-controlling protein {ECO:0000255|HAMAP-Rule:MF_01664};
GN Name=ctaA {ECO:0000255|HAMAP-Rule:MF_01664}; OrderedLocusNames=Exig_1990;
OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS 255-15).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=262543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of heme O to heme A by two
CC successive hydroxylations of the methyl group at C8. The first
CC hydroxylation forms heme I, the second hydroxylation results in an
CC unstable dihydroxymethyl group, which spontaneously dehydrates,
CC resulting in the formyl group of heme A. {ECO:0000255|HAMAP-
CC Rule:MF_01664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a;
CC Xref=Rhea:RHEA:63388, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:60530, ChEBI:CHEBI:61715;
CC EC=1.17.99.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01664};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63389;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01664};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01664};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; heme A biosynthesis;
CC heme A from heme O: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01664}.
CC -!- SUBUNIT: Interacts with CtaB. {ECO:0000255|HAMAP-Rule:MF_01664}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01664};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01664}.
CC -!- SIMILARITY: Belongs to the COX15/CtaA family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01664}.
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DR EMBL; CP001022; ACB61442.1; -; Genomic_DNA.
DR RefSeq; WP_012370860.1; NC_010556.1.
DR AlphaFoldDB; B1YIW6; -.
DR SMR; B1YIW6; -.
DR STRING; 262543.Exig_1990; -.
DR EnsemblBacteria; ACB61442; ACB61442; Exig_1990.
DR KEGG; esi:Exig_1990; -.
DR eggNOG; COG1612; Bacteria.
DR HOGENOM; CLU_041525_3_0_9; -.
DR OMA; YTGAYVR; -.
DR OrthoDB; 1135592at2; -.
DR UniPathway; UPA00269; UER00713.
DR Proteomes; UP000001681; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016653; F:oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor; IEA:InterPro.
DR GO; GO:0006784; P:heme A biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01664; HemeA_synth_type1; 1.
DR InterPro; IPR003780; COX15/CtaA_fam.
DR InterPro; IPR023755; HemeA_Synthase_type1.
DR Pfam; PF02628; COX15-CtaA; 1.
PE 3: Inferred from homology;
KW Cell membrane; Heme biosynthesis; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..297
FT /note="Heme A synthase"
FT /id="PRO_0000348978"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT BINDING 208
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT BINDING 268
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
SQ SEQUENCE 297 AA; 33310 MW; 26FB932A135EA84F CRC64;
MNRKLSIFSA FVTFTMMIVL LMGGTVTKTD SGNGCGTDWP LCHGELIPTN PSVETMIEYS
HRAVTGVVGL LIIALCLWTL VAFKDRLDIK IFAFLAFIFM LIQSIVGAGA VVWQQSDLVM
ALHFGISLIS FASLLILTIL IMERSGQEFR ESVPAFLRKL LYGLLIYTLI VVYTGAFVRH
VGATYACVGW PVCSQPTMTF EAWVQMIHRI LAGLLFFYTL FVHYTAIRLK HRTSRTGMLF
ATFFISCQVA TGAWIVLGGH ATYVPLLHAF LITCYFGVIS YLAYHAFRTR KKDSRLR
