ID   CTAA_BRUAB              Reviewed;         358 AA.
AC   Q57DW5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 87.
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};
GN   OrderedLocusNames=BruAb1_0801;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; Evidence={ECO:0000255|HAMAP-
CC         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; AE017223; AAX74169.1; -; Genomic_DNA.
DR   RefSeq; WP_002969419.1; NC_006932.1.
DR   AlphaFoldDB; Q57DW5; -.
DR   SMR; Q57DW5; -.
DR   EnsemblBacteria; AAX74169; AAX74169; BruAb1_0801.
DR   GeneID; 55590500; -.
DR   KEGG; bmb:BruAb1_0801; -.
DR   HOGENOM; CLU_017627_0_0_5; -.
DR   UniPathway; UPA00269; UER00713.
DR   Proteomes; UP000000540; Chromosome I.
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; CYTOCHROME C OXIDASE ASSEMBLY PROTEIN COX15; 1.
DR   PANTHER; PTHR23289:SF2; CYTOCHROME C OXIDASE ASSEMBLY PROTEIN COX15 HOMOLOG; 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..358
FT                   /note="Heme A synthase"
FT                   /id="PRO_0000349020"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   BINDING         273
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         334
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   358 AA;  40048 MW;  4DF7F2FBFAF09798 CRC64;
     MAATSAQHIG LQGHGTSRND RDRRLVRYWL YAVFAVLIAI VMVGGATRMT GSGLSITEWK
     PIHGVIPPLN HAEWVEEFEK YQQIPQYQQI NKGMSLAEFQ YIFWWEWAHR LLARFVGFLV
     AVPLGFFWLT GRLKGGLKYR MLGLLALGGL QGAIGWWMVA SGLSELTSVS QYRLAIHLTT
     ACVIITAVFY IARGLVTYSE RPAERSIQRF AGWIVFAVLV QIYLGGLVAG LHAGLTYNTW
     PLMDGAIIPS DLFTQAPWWR NLFENPKTVQ FVHRMFAYTV LLLAILHAVQ VWKNAPGTTH
     ARRTIVLVGL VFIQAMIGIA TLLMSAPLHL GLTHQFFALV VLAFAVAHWR ATKGAYAA
//