CTAA_METPB
ID CTAA_METPB Reviewed; 381 AA.
AC B1ZGD8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Mpop_1632;
OS Methylorubrum populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
OS (Methylobacterium populi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=441620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-705 / NCIMB 13946 / BJ001;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium populi BJ001.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001029; ACB79796.1; -; Genomic_DNA.
DR RefSeq; WP_012453543.1; NC_010725.1.
DR AlphaFoldDB; B1ZGD8; -.
DR SMR; B1ZGD8; -.
DR STRING; 441620.Mpop_1632; -.
DR EnsemblBacteria; ACB79796; ACB79796; Mpop_1632.
DR KEGG; mpo:Mpop_1632; -.
DR eggNOG; COG1612; Bacteria.
DR HOGENOM; CLU_017627_0_0_5; -.
DR OMA; YWWEWGH; -.
DR UniPathway; UPA00269; UER00713.
DR Proteomes; UP000007136; 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..381
FT /note="Heme A synthase"
FT /id="PRO_0000349045"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 138..158
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 212..232
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT BINDING 277
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 337
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 381 AA; 40425 MW; 84DE3278D5D8798E CRC64;
MRLSKAPPAD RFDAVPAASD RPGRGAVRAW LYLLAVLVVA MVAVGGATRL TGSGLSITEW
RPVTGVVPPL NAADWAVEFD KYRDTPQYRI LNQGIGLDGF KTLYWWEWGH RLLGRIVGLV
FFLPFAWFWW RGWLGRRLLL GLLGLGLLGG LQGAIGWIMV ASGLQPGMTA VAPLKLALHL
TTASLILAGL VWLAAGTRAL ALAPAPEPVR RVAGLLPVLV LIQIWLGGLV AGSKAGLLYN
TWPDMDGMLV PPARMLFDKV PFIENFVDNL ALVQFNHRLF AYLVVLVALA HAVQAVRMAP
GAAAGRAMGV AALTLAQMGL GIVTLLLQVP LWAGLAHQVF AMAVLIMATV HARLSVGVPA
ASAPTGAAVP IGLEALAGRG V
