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Database: UniProt
Entry: A8H803_SHEPA
LinkDB: A8H803_SHEPA
Original site: A8H803_SHEPA 
ID   A8H803_SHEPA            Unreviewed;       205 AA.
AC   A8H803;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   24-JAN-2024, entry version 82.
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=Spea_3376 {ECO:0000313|EMBL:ABV88690.1};
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579 {ECO:0000313|EMBL:ABV88690.1, ECO:0000313|Proteomes:UP000002608};
RN   [1] {ECO:0000313|EMBL:ABV88690.1, ECO:0000313|Proteomes:UP000002608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1 {ECO:0000313|Proteomes:UP000002608};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-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; CP000851; ABV88690.1; -; Genomic_DNA.
DR   RefSeq; WP_012156589.1; NC_009901.1.
DR   AlphaFoldDB; A8H803; -.
DR   STRING; 398579.Spea_3376; -.
DR   KEGG; spl:Spea_3376; -.
DR   eggNOG; COG2109; Bacteria.
DR   HOGENOM; CLU_088595_0_0_6; -.
DR   OMA; HAMGEGF; -.
DR   OrthoDB; 9810309at2; -.
DR   UniPathway; UPA00148; UER00233.
DR   Proteomes; UP000002608; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000002608};
KW   Transferase {ECO:0000256|PIRNR:PIRNR015617, ECO:0000313|EMBL:ABV88690.1}.
FT   DOMAIN          11..30
FT                   /note="Cob(I)alamin adenosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12557"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   205 AA;  22691 MW;  AC921CC061B0ACBD CRC64;
     MTQEKSTDAI KAERHKARQQ RIKEGVDAKI ARAQEEKGIL LVLTGNGKGK STSGFGTVVR
     AVGHGKKAAV VQFIKGNWDC GERTLLEGAG VEFHVMGTGF TWETQDREKD TAAAVKAWEA
     TEKLLKDETI DLVMLDELTY MVSYHYLEVE RVIEALKNRP PMQHVIVTGR ACHRAIVDLA
     DTVSEVQPVK HAFEAGIKAQ PGFDY
//
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