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Database: UniProt
Entry: F3LHC9_9GAMM
LinkDB: F3LHC9_9GAMM
Original site: F3LHC9_9GAMM 
ID   F3LHC9_9GAMM            Unreviewed;       197 AA.
AC   F3LHC9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Corrinoid adenosyltransferase {ECO:0000256|ARBA:ARBA00012454, ECO:0000256|PIRNR:PIRNR015617};
DE            EC=2.5.1.17 {ECO:0000256|ARBA:ARBA00012454, ECO:0000256|PIRNR:PIRNR015617};
DE   AltName: Full=Cob(II)alamin adenosyltransferase {ECO:0000256|PIRNR:PIRNR015617};
DE   AltName: Full=Cob(II)yrinic acid a,c-diamide adenosyltransferase {ECO:0000256|PIRNR:PIRNR015617};
GN   ORFNames=IMCC1989_896 {ECO:0000313|EMBL:EGG93701.1};
OS   gamma proteobacterium IMCC1989.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX   NCBI_TaxID=937772 {ECO:0000313|EMBL:EGG93701.1, ECO:0000313|Proteomes:UP000010300};
RN   [1] {ECO:0000313|EMBL:EGG93701.1, ECO:0000313|Proteomes:UP000010300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC1989 {ECO:0000313|EMBL:EGG93701.1,
RC   ECO:0000313|Proteomes:UP000010300};
RX   PubMed=21602334; DOI=10.1128/JB.05202-11;
RA   Jang Y., Oh H.M., Kim H., Kang I., Cho J.C.;
RT   "Genome sequence of strain IMCC1989, a novel member of the marine
RT   gammaproteobacteria.";
RL   J. Bacteriol. 193:3672-3673(2011).
CC   -!- FUNCTION: Required for both de novo synthesis of the corrin ring for
CC       the assimilation of exogenous corrinoids. Participates in the
CC       adenosylation of a variety of incomplete and complete corrinoids.
CC       {ECO:0000256|ARBA:ARBA00024929, ECO:0000256|PIRNR:PIRNR015617}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + 2 cob(II)alamin + reduced [electron-transfer
CC         flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized
CC         [electron-transfer flavoprotein] + 2 triphosphate;
CC         Xref=Rhea:RHEA:28671, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16304, ChEBI:CHEBI:18036,
CC         ChEBI:CHEBI:18408, ChEBI:CHEBI:30616, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307; EC=2.5.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00001328,
CC         ECO:0000256|PIRNR:PIRNR015617};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + 2 cob(II)yrinate a,c diamide + reduced [electron-
CC         transfer flavoprotein] = 2 adenosylcob(III)yrinate a,c-diamide + 3
CC         H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate;
CC         Xref=Rhea:RHEA:11528, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:18036, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:58503,
CC         ChEBI:CHEBI:58537; EC=2.5.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00000143,
CC         ECO:0000256|PIRNR:PIRNR015617};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
CC       {ECO:0000256|ARBA:ARBA00005121, ECO:0000256|PIRNR:PIRNR015617}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR015617}.
CC   -!- SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00007487, ECO:0000256|PIRNR:PIRNR015617}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGG93701.1}.
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DR   EMBL; AEVK01000173; EGG93701.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3LHC9; -.
DR   OrthoDB; 9810309at2; -.
DR   UniPathway; UPA00148; UER00233.
DR   Proteomes; UP000010300; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008817; F:corrinoid adenosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00561; CobA_ACA; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003724; CblAdoTrfase_CobA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00708; cobA; 1.
DR   PANTHER; PTHR46638; CORRINOID ADENOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR46638:SF1; CORRINOID ADENOSYLTRANSFERASE; 1.
DR   Pfam; PF02572; CobA_CobO_BtuR; 1.
DR   PIRSF; PIRSF015617; Adensltrnsf_CobA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR015617};
KW   Cobalamin biosynthesis {ECO:0000256|PIRNR:PIRNR015617};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR015617};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR015617};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW   ECO:0000256|PIRNR:PIRNR015617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010300};
KW   Transferase {ECO:0000256|PIRNR:PIRNR015617, ECO:0000313|EMBL:EGG93701.1}.
SQ   SEQUENCE   197 AA;  22454 MW;  021CE22BFF74488E CRC64;
     MTDQEHKQRM IKRKEVMDAK IAKATEERGV LILLKGNGKG KSSSAFGTML RSVGHGKKCA
     VIQFIKGRSE TGEYKFFKDH PQVEWHVMGH GFTWETQDKE QDIKAAQQAW AVAEKLLQDD
     SYDMLVFDEM SYMFKYDYLD VAPVVAALQQ RPKKQNVIIT GRTMALPLQD IADTISVVQD
     ERHAFRLGVK AQIGIEY
//
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