CTAA_EHRCR
ID CTAA_EHRCR Reviewed; 344 AA.
AC Q2GHG8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, 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}; OrderedLocusNames=ECH_0294;
OS Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=205920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC CRL-10679 / Arkansas;
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
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; CP000236; ABD45450.1; -; Genomic_DNA.
DR RefSeq; WP_011452517.1; NC_007799.1.
DR AlphaFoldDB; Q2GHG8; -.
DR SMR; Q2GHG8; -.
DR STRING; 205920.ECH_0294; -.
DR EnsemblBacteria; ABD45450; ABD45450; ECH_0294.
DR KEGG; ech:ECH_0294; -.
DR eggNOG; COG1612; Bacteria.
DR HOGENOM; CLU_017627_0_0_5; -.
DR OMA; YWWEWGH; -.
DR OrthoDB; 1135592at2; -.
DR UniPathway; UPA00269; UER00713.
DR Proteomes; UP000008320; 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; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..344
FT /note="Heme A synthase"
FT /id="PRO_0000349031"
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 198..218
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 287..307
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT BINDING 262
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 317
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 344 AA; 39512 MW; BA66FE56E06A7553 CRC64;
MKIASDNREV CVGVKIWLCI CCIGILLMVL VGGITRLTHS GLSITEWNPV IGVFPPIGER
AWIREKIKYM ATPEFKYLNF NITLRGFRKL YLIEYFHRLL GRIVGLTFLI PFLYFTYKKK
LHRNLIINFI VICLLILFQG VVGWFMVKSG LIDRPHVSHY KLTAHLLLAL LIFYLLWRQF
LLSTISKVTY NIKVNGTLIF SVISVLIVTQ ITFGSLVAGL NAGLLDKTIP FLAGKLMLED
LLFIKPLWYN IFENPVTVQF IHELIATLIF LVVIITLLIL RLNLFPAYLL LICLCLQLTL
GVLTFIYNVP IVLASLHQVT AFILFAVNTY LLHYMKLSKL QYVK
