位置:首页 > 蛋白库 > CTAA_METC4
CTAA_METC4
ID   CTAA_METC4              Reviewed;         382 AA.
AC   B7KV80;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=Mchl_1888;
OS   Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS   extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=440085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM4 / NCIMB 13688;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., 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., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Marx C., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT   CM4.";
RL   Submitted (DEC-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}.
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; CP001298; ACK82751.1; -; Genomic_DNA.
DR   RefSeq; WP_015950506.1; NC_011757.1.
DR   AlphaFoldDB; B7KV80; -.
DR   SMR; B7KV80; -.
DR   PRIDE; B7KV80; -.
DR   EnsemblBacteria; ACK82751; ACK82751; Mchl_1888.
DR   KEGG; mch:Mchl_1888; -.
DR   HOGENOM; CLU_017627_0_0_5; -.
DR   OMA; YWWEWGH; -.
DR   BioCyc; MEXT440085:MCHL_RS09115-MON; -.
DR   UniPathway; UPA00269; UER00713.
DR   Proteomes; UP000002385; 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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..382
FT                   /note="Heme A synthase"
FT                   /id="PRO_1000187251"
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        141..161
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        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01665"
FT   TRANSMEM        327..347
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         338
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   382 AA;  40276 MW;  C2CCE1C87469B804 CRC64;
     MRLSTNPTLD RFDAVPAASY RPGHGAVRAW LYLLAVLVVA MVAVGGATRL TGSGLSITEW
     RPVTGVVPPL DAADWAVEFD KYRDTPQYRI LNQGIGLDGF KTLYWWEWGH RLLGRIVGLV
     FFLPFAWFWA RGMLGRRLLT GLLGLGLLGG LQGAIGWIMV ASGLQPGMTA VAPLKLALHL
     TTASLILAGL VWLAAGTRPR ALAPAPESVR VVACLLPALV LVQIWLGGLV AGSKAGLLYN
     TWPDMDGVLV PPARVLFDKV PFIENFIDNL ALVQFNHRLF AYLVVAVAIA HAIQAARTAS
     GSAAAGRAMG VAALATAQMG LGIATLLLHV PLWAGLAHQV FAMAVLIMAT VHARLARGVP
     AAAAPTGAEV PIGLEALAGR GA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024