PUCG_BACSU
ID PUCG_BACSU Reviewed; 416 AA.
AC O32148;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=(S)-ureidoglycine--glyoxylate transaminase {ECO:0000305};
DE Short=UGXT {ECO:0000303|PubMed:20852637};
DE EC=2.6.1.112 {ECO:0000269|PubMed:20852637};
DE AltName: Full=(S)-ureidoglycine--glyoxylate aminotransferase {ECO:0000303|PubMed:20852637};
DE AltName: Full=Purine catabolism protein PucG {ECO:0000305};
GN Name=pucG {ECO:0000303|PubMed:11344136}; Synonyms=yurG;
GN OrderedLocusNames=BSU32520;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP INDUCTION, AND PATHWAY.
RC STRAIN=168;
RX PubMed=11344136; DOI=10.1128/jb.183.11.3293-3302.2001;
RA Schultz A.C., Nygaard P., Saxild H.H.;
RT "Functional analysis of 14 genes that constitute the purine catabolic
RT pathway in Bacillus subtilis and evidence for a novel regulon controlled by
RT the PucR transcription activator.";
RL J. Bacteriol. 183:3293-3302(2001).
RN [3] {ECO:0007744|PDB:3ISL}
RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, COFACTOR, PATHWAY,
RP SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-198, AND MUTAGENESIS OF GLN-37 AND
RP ASN-264.
RX PubMed=20852637; DOI=10.1038/nchembio.445;
RA Ramazzina I., Costa R., Cendron L., Berni R., Peracchi A., Zanotti G.,
RA Percudani R.;
RT "An aminotransferase branch point connects purine catabolism to amino acid
RT recycling.";
RL Nat. Chem. Biol. 6:801-806(2010).
CC -!- FUNCTION: Catalyzes the transamination between an unstable intermediate
CC ((S)-ureidoglycine) and the end product of purine catabolism
CC (glyoxylate) to yield oxalurate and glycine. Glyoxylate is the
CC preferred substrate, but other amino-group acceptors can be used.
CC {ECO:0000269|PubMed:20852637}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2-ureidoglycine + glyoxylate = glycine + N-carbamoyl-2-
CC oxoglycine; Xref=Rhea:RHEA:33867, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57824, ChEBI:CHEBI:59947;
CC EC=2.6.1.112; Evidence={ECO:0000269|PubMed:20852637};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:20852637};
CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation.
CC {ECO:0000305|PubMed:11344136, ECO:0000305|PubMed:20852637}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20852637}.
CC -!- INDUCTION: Expression is very low in excess nitrogen (glutamate plus
CC ammonia) and is induced during limiting-nitrogen conditions
CC (glutamate). Expression is further induced when allantoin is added
CC during limiting-nitrogen conditions. {ECO:0000269|PubMed:11344136}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AL009126; CAB15242.1; -; Genomic_DNA.
DR PIR; F70017; F70017.
DR RefSeq; NP_391132.1; NC_000964.3.
DR RefSeq; WP_003244520.1; NZ_JNCM01000033.1.
DR PDB; 3ISL; X-ray; 2.06 A; A/B=1-416.
DR PDBsum; 3ISL; -.
DR AlphaFoldDB; O32148; -.
DR SMR; O32148; -.
DR STRING; 224308.BSU32520; -.
DR PaxDb; O32148; -.
DR PRIDE; O32148; -.
DR EnsemblBacteria; CAB15242; CAB15242; BSU_32520.
DR GeneID; 936676; -.
DR KEGG; bsu:BSU32520; -.
DR PATRIC; fig|224308.43.peg.3402; -.
DR eggNOG; COG0075; Bacteria.
DR InParanoid; O32148; -.
DR OMA; IRINHMG; -.
DR PhylomeDB; O32148; -.
DR BioCyc; BSUB:BSU32520-MON; -.
DR UniPathway; UPA00395; -.
DR EvolutionaryTrace; O32148; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IBA:GO_Central.
DR GO; GO:0004760; F:serine-pyruvate transaminase activity; IBA:GO_Central.
DR GO; GO:0000256; P:allantoin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IBA:GO_Central.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Purine metabolism; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..416
FT /note="(S)-ureidoglycine--glyoxylate transaminase"
FT /id="PRO_0000150244"
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:20852637"
FT MUTAGEN 37
FT /note="Q->H: 5-fold decrease in transamination activity."
FT /evidence="ECO:0000269|PubMed:20852637"
FT MUTAGEN 264
FT /note="N->S: 9-fold decrease in transamination activity."
FT /evidence="ECO:0000269|PubMed:20852637"
FT MUTAGEN 264
FT /note="N->Y: Loss of transamination activity."
FT /evidence="ECO:0000269|PubMed:20852637"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 40..56
FT /evidence="ECO:0007829|PDB:3ISL"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:3ISL"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:3ISL"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:3ISL"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:3ISL"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:3ISL"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:3ISL"
FT TURN 174..179
FT /evidence="ECO:0007829|PDB:3ISL"
FT TURN 184..188
FT /evidence="ECO:0007829|PDB:3ISL"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:3ISL"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:3ISL"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 270..286
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 288..308
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3ISL"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 335..346
FT /evidence="ECO:0007829|PDB:3ISL"
FT TURN 356..360
FT /evidence="ECO:0007829|PDB:3ISL"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 373..389
FT /evidence="ECO:0007829|PDB:3ISL"
FT HELIX 398..408
FT /evidence="ECO:0007829|PDB:3ISL"
SQ SEQUENCE 416 AA; 45743 MW; D0181DFADEADB9D4 CRC64;
MSGRRELCTP LRTIMTPGPV EVDPRVLRVM STPVVGQFDP AFTGIMNETM EMLRELFQTK
NRWAYPIDGT SRAGIEAVLA SVIEPEDDVL IPIYGRFGYL LTEIAERYGA NVHMLECEWG
TVFDPEDIIR EIKKVKPKIV AMVHGETSTG RIHPLKAIGE ACRTEDALFI VDAVATIGGC
EVKVDEWKID AAIGGTQKCL SVPSGMAPIT YNERVADVIA ARKKVERGIA TQADRAALSG
NRPITSNYFD LSQLEDYWSE RRLNHHTEAT TMLYALREGV RLVLEEGLET RFERHRHHEA
ALAAGIKAMG LRLFGDDSCK MPVVTCVEIP GGIDGESVRD MLLAQFGIEI ASSFGPLAGK
IWRIGTMGYS CRKENVLFVL AGLEAVLLRH NAGIEAGKAL QAALDVYENA GRQAAV
