ID A4Y9N9_SHEPC Unreviewed; 207 AA.
AC A4Y9N9;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
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 OrderedLocusNames=Sputcn32_2957 {ECO:0000313|EMBL:ABP76672.1};
OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP76672.1};
RN [1] {ECO:0000313|EMBL:ABP76672.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN-32 {ECO:0000313|EMBL:ABP76672.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella putrefaciens CN-32.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000681; ABP76672.1; -; Genomic_DNA.
DR AlphaFoldDB; A4Y9N9; -.
DR STRING; 319224.Sputcn32_2957; -.
DR KEGG; spc:Sputcn32_2957; -.
DR eggNOG; COG2109; Bacteria.
DR HOGENOM; CLU_088595_0_0_6; -.
DR UniPathway; UPA00148; UER00233.
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; IPR025826; Co_AT_N_dom.
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; PF12557; Co_AT_N; 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 Transferase {ECO:0000256|PIRNR:PIRNR015617, ECO:0000313|EMBL:ABP76672.1}.
FT DOMAIN 13..32
FT /note="Cob(I)alamin adenosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12557"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 207 AA; 22681 MW; B14C1CFB4C521C82 CRC64;
MTAQNDNEQA QIKAERHKAR QQKVKAGVDA KIAAAQEEKG ILLVLTGNGK GKSTSGFGTV
ARAVGHGKKA AVVQFIKGTW ECGERNLLEG AGVEFHVMGT GFTWETQDKE KDTAAAVLAW
EAAEKLLQDE SIDCVMLDEL TYMVSYHYLD VERVLSALKN RPPMQHVIIT GRACHRAIIE
LADTVSEVQP LKHAFESGIK AQQGFDY
//
