CTAA_WOLPM
ID CTAA_WOLPM Reviewed; 350 AA.
AC Q73HV8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Heme A synthase {ECO:0000255|HAMAP-Rule:MF_01665};
DE Short=HAS {ECO:0000255|HAMAP-Rule:MF_01665};
DE EC=1.17.99.9 {ECO:0000255|HAMAP-Rule:MF_01665};
DE AltName: Full=Cytochrome aa3-controlling protein {ECO:0000255|HAMAP-Rule:MF_01665};
GN Name=ctaA {ECO:0000255|HAMAP-Rule:MF_01665}; OrderedLocusNames=WD_0432;
OS Wolbachia pipientis wMel.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=163164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T., Brownlie J.C.,
RA McGraw E.A., Martin W., Esser C., Ahmadinejad N., Wiegand C., Madupu R.,
RA Beanan M.J., Brinkac L.M., Daugherty S.C., Durkin A.S., Kolonay J.F.,
RA Nelson W.C., Mohamoud Y., Lee P., Berry K.J., Young M.B., Utterback T.R.,
RA Weidman J.F., Nierman W.C., Paulsen I.T., Nelson K.E., Tettelin H.,
RA O'Neill S.L., Eisen J.A.;
RT "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a
RT streamlined genome overrun by mobile genetic elements.";
RL PLoS Biol. 2:327-341(2004).
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_01665}.
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_01665};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63389;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01665};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01665};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; heme A biosynthesis;
CC heme A from heme O: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01665}.
CC -!- SUBUNIT: Interacts with CtaB. {ECO:0000255|HAMAP-Rule:MF_01665}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01665};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01665}.
CC -!- SIMILARITY: Belongs to the COX15/CtaA family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01665}.
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DR EMBL; AE017196; AAS14155.1; -; Genomic_DNA.
DR AlphaFoldDB; Q73HV8; -.
DR SMR; Q73HV8; -.
DR STRING; 163164.WD_0432; -.
DR EnsemblBacteria; AAS14155; AAS14155; WD_0432.
DR KEGG; wol:WD_0432; -.
DR eggNOG; COG1612; Bacteria.
DR OMA; YWWEWGH; -.
DR UniPathway; UPA00269; UER00713.
DR Proteomes; UP000008215; 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_01665; HemeA_synth_type2; 1.
DR InterPro; IPR003780; COX15/CtaA_fam.
DR InterPro; IPR023754; HemeA_Synthase_type2.
DR PANTHER; PTHR23289; PTHR23289; 1.
DR Pfam; PF02628; COX15-CtaA; 1.
PE 3: Inferred from homology;
KW Cell membrane; Heme biosynthesis; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..350
FT /note="Heme A synthase"
FT /id="PRO_0000349087"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT BINDING 264
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_01665"
FT BINDING 318
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_01665"
SQ SEQUENCE 350 AA; 39906 MW; EA0CCBCD2B434FE3 CRC64;
MEQNSAWFME AKPVAIWLFL CSVMVILMVG IGGFTRLSKA GLSITEWKPI TGTLPPLSEQ
DWLQEKLKYE ATPEYKALNY GISMEEFRAI YLIEYVHRLV ARLTGLVFVL PFIYFTLRRK
ISKKVVIKLF VALLFGALQA FAGWYMVKSG LVAKPHVSHY RLALHLLLAL IIFALFSYQF
FDYQIRPKQT KLKISCNTKY YVGIILVLIM IQIIFGAFVA GLNAGLIYNT FPLMDGQIVP
EDLFFLQPTW LNIFENRATV QFIHRALALL ILTLVVILTV KNASIKPVYI MLLSVIIQII
LGVITLLLHI PIAIAIAHQV FSFILFGSSL YFLCYLRKQT TSPICTFFPS
