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Database: UniProt
Entry: A6VM62_ACTSZ
LinkDB: A6VM62_ACTSZ
Original site: A6VM62_ACTSZ 
ID   A6VM62_ACTSZ            Unreviewed;       393 AA.
AC   A6VM62;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   24-JAN-2024, entry version 109.
DE   RecName: Full=Formate-dependent phosphoribosylglycinamide formyltransferase {ECO:0000256|HAMAP-Rule:MF_01643};
DE            EC=6.3.1.21 {ECO:0000256|HAMAP-Rule:MF_01643};
DE   AltName: Full=5'-phosphoribosylglycinamide transformylase 2 {ECO:0000256|HAMAP-Rule:MF_01643};
DE   AltName: Full=Formate-dependent GAR transformylase {ECO:0000256|HAMAP-Rule:MF_01643};
DE   AltName: Full=GAR transformylase 2 {ECO:0000256|HAMAP-Rule:MF_01643};
DE            Short=GART 2 {ECO:0000256|HAMAP-Rule:MF_01643};
DE   AltName: Full=Non-folate glycinamide ribonucleotide transformylase {ECO:0000256|HAMAP-Rule:MF_01643};
DE   AltName: Full=Phosphoribosylglycinamide formyltransferase 2 {ECO:0000256|HAMAP-Rule:MF_01643};
GN   Name=purT {ECO:0000256|HAMAP-Rule:MF_01643};
GN   OrderedLocusNames=Asuc_0686 {ECO:0000313|EMBL:ABR74059.1};
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671 {ECO:0000313|EMBL:ABR74059.1, ECO:0000313|Proteomes:UP000001114};
RN   [1] {ECO:0000313|Proteomes:UP000001114}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z
RC   {ECO:0000313|Proteomes:UP000001114};
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
CC   -!- FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes the
CC       transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing
CC       5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by
CC       PurU via hydrolysis of 10-formyl-tetrahydrofolate. {ECO:0000256|HAMAP-
CC       Rule:MF_01643}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + formate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide =
CC         ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide +
CC         phosphate; Xref=Rhea:RHEA:24829, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:456216;
CC         EC=6.3.1.21; Evidence={ECO:0000256|HAMAP-Rule:MF_01643};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-
CC       formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-
CC       ribosyl)glycinamide (formate route): step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01643}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01643}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000256|HAMAP-
CC       Rule:MF_01643}.
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DR   EMBL; CP000746; ABR74059.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VM62; -.
DR   STRING; 339671.Asuc_0686; -.
DR   KEGG; asu:Asuc_0686; -.
DR   eggNOG; COG0027; Bacteria.
DR   HOGENOM; CLU_011534_1_3_6; -.
DR   OMA; GMVTMIT; -.
DR   OrthoDB; 9804625at2; -.
DR   UniPathway; UPA00074; UER00127.
DR   Proteomes; UP000001114; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0043815; F:phosphoribosylglycinamide formyltransferase 2 activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   HAMAP; MF_01643; PurT; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR005862; PurT.
DR   InterPro; IPR048740; PurT_C.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   NCBIfam; TIGR01142; purT; 1.
DR   PANTHER; PTHR43055; FORMATE-DEPENDENT PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR   PANTHER; PTHR43055:SF1; FORMATE-DEPENDENT PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   Pfam; PF21244; PurT_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01643}; Ligase {ECO:0000256|HAMAP-Rule:MF_01643};
KW   Lyase {ECO:0000313|EMBL:ABR74059.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01643};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01643};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01643, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01643}; Reference proteome {ECO:0000313|Proteomes:UP000001114};
KW   Transferase {ECO:0000313|EMBL:ABR74059.1}.
FT   DOMAIN          119..308
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   BINDING         22..23
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         82
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         114
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         155
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         160..165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         195..198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         279
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         286
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         356
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
FT   BINDING         363..364
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01643"
SQ   SEQUENCE   393 AA;  42604 MW;  ABD61B8CBDDB4484 CRC64;
     MATIGTALTA KATKVMLLGA GELGKEVAIE LMRFGVEVIA VDRYEQAPAQ QVAHRAYTIS
     MLDGSALRAL VEKERPDYIV PEVEAIATDT LVELEQEGFT VVPTAKATML TMNREGIRRL
     AAEELALPTS PYQFVDNFTD FQSAVEKIGV PCVVKPIMSS SGHGQSVIKS LADAERAWHY
     AQEGGRAGGG RVIVEGFVKF DYEITLLTVR HIGGTSFLAP IGHRQEDGDY RESWQPQAMS
     EAALKKARNV AEKITTALGG RGIFGVEMFV CGDDVIFNEV SPRPHDTGMV TLISQELSEF
     ALHARAILGL PIPTINLISP AASKAVVVEG QSNQVQFGNL DKVLAEANTD LRIFGKGEVN
     GHRRMAVILS RDISVEKALE KASRAYARLQ ISL
//
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