CTAA_PARL1
ID CTAA_PARL1 Reviewed; 344 AA.
AC A7HXA1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Plav_2927;
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966;
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(2011).
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; CP000774; ABS64534.1; -; Genomic_DNA.
DR RefSeq; WP_012111850.1; NC_009719.1.
DR AlphaFoldDB; A7HXA1; -.
DR SMR; A7HXA1; -.
DR STRING; 402881.Plav_2927; -.
DR EnsemblBacteria; ABS64534; ABS64534; Plav_2927.
DR KEGG; pla:Plav_2927; -.
DR eggNOG; COG1612; Bacteria.
DR HOGENOM; CLU_017627_0_0_5; -.
DR OMA; YWWEWGH; -.
DR OrthoDB; 1135592at2; -.
DR UniPathway; UPA00269; UER00713.
DR Proteomes; UP000006377; 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_0000349058"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 265..285
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 267
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 324
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; 38529 MW; C8A5BA8DF72E53A0 CRC64;
MNILPRINAI EKTDANHHAI AWWLIGVAAL VFIMVVVGGL TRLTESGLSI TEWKPVTGAL
PPMTEEHWQE EFDLYRQIPQ YQLVNKGMSL DEFKTIYWWE WSHRFLGRLI GLAFFVPFVF
FVVTRRVERA LVPRLIFLFV LGGMQGVLGW WMVMSGLTDR TEVSQYRLAA HLGLATLIFG
ALIWTALDLL NGKSTRLLTG LAKAAAAILA LIFLQTILGA FVAGIRAGLI YNTWPLMAGA
FIPDGLFAMT PVWHNFFESH LTVQFQHRMT AYLLLLCVVW HWWAARKTAA APSAGWLAVA
TFAQACIGIW TVLWVVPIPL GAAHQAGAMV VFGVAVWHVH RLAK
