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CTAA_BART1
ID   CTAA_BART1              Reviewed;         358 AA.
AC   A9IVC8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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}; Synonyms=cox15;
GN   OrderedLocusNames=BT_1320;
OS   Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=382640;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 105476 / IBS 506;
RX   PubMed=18037886; DOI=10.1038/ng.2007.38;
RA   Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA   Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT   "Genomic analysis of Bartonella identifies type IV secretion systems as
RT   host adaptability factors.";
RL   Nat. Genet. 39:1469-1476(2007).
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; AM260525; CAK01684.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9IVC8; -.
DR   SMR; A9IVC8; -.
DR   STRING; 382640.BT_1320; -.
DR   EnsemblBacteria; CAK01684; CAK01684; BT_1320.
DR   KEGG; btr:BT_1320; -.
DR   eggNOG; COG1612; Bacteria.
DR   HOGENOM; CLU_017627_0_0_5; -.
DR   OMA; YWWEWGH; -.
DR   UniPathway; UPA00269; UER00713.
DR   Proteomes; UP000001592; 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..358
FT                   /note="Heme A synthase"
FT                   /id="PRO_0000349015"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        208..228
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        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   BINDING         271
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         332
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;  40910 MW;  62FBA5DF92F9E3BC CRC64;
     MAVKRLNDNL LTPVQKRNRK QIQVWLYSIL LLCLAIVLVG GATRLTGSGL SITEWKPIHG
     VIPPIGVEQW QEEFLKYQQI TQYKLLNRDM TLSAFKVIFW WEWAHRVLGR LVGLVALLGL
     IWFWATKRIE KNILFPLIVV PILIAFQGFI GWWMVASGIG QSNLTSVSQY RLAFHLITAC
     LVIIFVTYLS RGLTEYSEKP ANQKVQCFAA WLVILVLIEI YLGALVAGLH AGKVYNTWPL
     MDGQIIPDGL LQHHPYWLNL FENPLTVQFI HRFFAYFLFI VSALHAFYVQ KNAPHSTHSR
     RAFLIFFIII IQAILGILTL LHEVPISLGL IHQSMALVVL CFAVAHWRAT KGAYRAVE
 
 
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