CTAA_GEOTD
ID CTAA_GEOTD Reviewed; 317 AA.
AC P94346;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 73.
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, ECO:0000303|PubMed:10052128};
OS Geobacillus thermodenitrificans.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=33940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K1041;
RX PubMed=8611588; DOI=10.1016/0005-2728(95)00126-3;
RA Kusano T., Kuge S., Sakamoto J., Noguchi S., Sone N.;
RT "Nucleotide and amino acid sequences for cytochrome caa3-type oxidase of
RT Bacillus stearothermophilus K1041 and non-Michaelis-type kinetics with
RT cytochrome c.";
RL Biochim. Biophys. Acta 1273:129-138(1996).
RN [2]
RP PROTEIN SEQUENCE OF 1-6, FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RC STRAIN=K1041;
RX PubMed=10052128; DOI=10.1271/bbb.63.96;
RA Sakamoto J., Hayakawa A., Uehara T., Noguchi S., Sone N.;
RT "Cloning of Bacillus stearothermophilus ctaA and heme A synthesis with the
RT CtaA protein produced in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 63:96-103(1999).
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, ECO:0000269|PubMed:10052128}.
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 ECO:0000269|PubMed:10052128};
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 ECO:0000305|PubMed:10052128}.
CC -!- SUBUNIT: Interacts with CtaB. {ECO:0000255|HAMAP-Rule:MF_01664}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01664,
CC ECO:0000269|PubMed:10052128}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01664}.
CC -!- SIMILARITY: Belongs to the COX15/CtaA family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01664, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA35111.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D70843; BAA35111.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; P94346; -.
DR SMR; P94346; -.
DR STRING; 33940.GTHT12_00517; -.
DR UniPathway; UPA00269; UER00713.
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 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Heme biosynthesis; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..317
FT /note="Heme A synthase"
FT /id="PRO_0000344244"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01664"
FT BINDING 213
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 275
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 317 AA; 35101 MW; A02214853B0C1D6A CRC64;
MQRSLKWFAS TTTVAMLFVL IGGALVTKTD SGMGCGRSWP LCHGQWIPDD ITPQLVIELS
HRLVSGLAAI MVLILCIRSW RVMGHVRETK PLAVLSFVFL VLQSLIGAAA VVWGQSDFVM
ALHFGISLIS FAAVLLLTLL IFVVDKKFSP TSLQLDGQMR FHIYGIIIYS YLVVYTGALV
RHTNASLACP SWPLCAKSRL LPVQFHEWVQ MGHRLAAAVI IIWIAVATVH AARYYREQPV
IYYGWIISLL LVLAQMVTGA LVVFTELNLY ISLAHAFFIS CLFGVLSYLL LLALRTRRRP
ATAAGRSVED TASAPLK
