CTAA_CERS4
ID CTAA_CERS4 Reviewed; 391 AA.
AC Q3IXW9; Q66LN8;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, 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, ECO:0000303|PubMed:15491161};
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};
GN Synonyms=cox15 {ECO:0000303|PubMed:15491161};
GN OrderedLocusNames=RHOS4_30470, RSP_3831;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH CTAB.
RX PubMed=15491161; DOI=10.1021/bi048469k;
RA Brown B.M., Wang Z., Brown K.R., Cricco J.A., Hegg E.L.;
RT "Heme O synthase and heme A synthase from Bacillus subtilis and Rhodobacter
RT sphaeroides interact in Escherichia coli.";
RL Biochemistry 43:13541-13548(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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, ECO:0000269|PubMed:15491161}.
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 ECO:0000269|PubMed:15491161}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01665,
CC ECO:0000305}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01665, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the COX15/CtaA family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01665, ECO:0000305}.
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DR EMBL; AY692269; AAU04881.1; -; Genomic_DNA.
DR EMBL; CP000144; ABA80615.1; -; Genomic_DNA.
DR RefSeq; WP_011338957.1; NZ_CP030272.1.
DR RefSeq; YP_354516.1; NC_007494.2.
DR AlphaFoldDB; Q3IXW9; -.
DR SMR; Q3IXW9; -.
DR IntAct; Q3IXW9; 1.
DR STRING; 272943.RSP_3831; -.
DR EnsemblBacteria; ABA80615; ABA80615; RSP_3831.
DR KEGG; rsp:RSP_3831; -.
DR PATRIC; fig|272943.9.peg.3418; -.
DR eggNOG; COG1612; Bacteria.
DR OMA; YWWEWGH; -.
DR PhylomeDB; Q3IXW9; -.
DR BRENDA; 1.17.99.9; 5383.
DR UniPathway; UPA00269; UER00713.
DR Proteomes; UP000002703; Chromosome 2.
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 1: Evidence at protein level;
KW Cell membrane; Heme biosynthesis; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..391
FT /note="Heme A synthase"
FT /id="PRO_0000344245"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT BINDING 300
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 360
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 391 AA; 43079 MW; F2981C94C40B1D83 CRC64;
MAVKKRSIFE EVGQGAKAPV PQGGSIDRGH GGARRGIRLW LMALFLLVMA MIVVGGLTRL
TDSGLSITEW RPVTGAVPPL NETQWAAEFD KYRDSPQYRL MNAGMTLAEF QRIYWWEWGH
RQLGRVIGLV WAVGFLGFLA ARRIPRGWWP RLLALGALGG LQGGIGWWMV ASGLEGDKVT
VESTRLATHL GLAFIILGLI AWQALLLGRS ESDLLQARRQ KDGRLVTLTT VLIGVAFLQI
VLGALVAGID AGRGFPTWPD MNGTFLPAEM FYVPGVETDW RNPAWWLGLL QNPGFVQFLH
RMAGYTLAAL GLIFWIFGRR SRHRATRGAF DLLAMALLAQ ILLGVGTVLS AAEWQVAIAH
QVGAVVIWVL ILHARHLALY PRVGSIRKGT L
