ID Q0BRB0_GRABC Unreviewed; 592 AA. AC Q0BRB0; DT 17-OCT-2006, integrated into UniProtKB/TrEMBL. DT 17-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 100. DE SubName: Full=Allophanate hydrolase {ECO:0000313|EMBL:ABI62642.1}; DE EC=3.5.1.54 {ECO:0000313|EMBL:ABI62642.1}; GN OrderedLocusNames=GbCGDNIH1_1744 {ECO:0000313|EMBL:ABI62642.1}; OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Granulibacter. OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI62642.1, ECO:0000313|Proteomes:UP000001963}; RN [1] {ECO:0000313|EMBL:ABI62642.1, ECO:0000313|Proteomes:UP000001963} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963}; RX PubMed=17827295; DOI=10.1128/JB.00793-07; RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E., RA Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.; RT "Genome sequence analysis of the emerging human pathogenic acetic acid RT bacterium Granulibacter bethesdensis."; RL J. Bacteriol. 189:8727-8736(2007). RN [2] {ECO:0007829|PDB:4GYR, ECO:0007829|PDB:4GYS} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS). RX PubMed=23282241; DOI=10.1021/bi301242m; RA Lin Y., St Maurice M.; RT "The structure of allophanate hydrolase from Granulibacter bethesdensis RT provides insights into substrate specificity in the amidase signature RT family."; RL Biochemistry 52:690-700(2013). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000394; ABI62642.1; -; Genomic_DNA. DR RefSeq; WP_011632446.1; NC_008343.2. DR PDB; 4GYR; X-ray; 2.80 A; A/B=1-592. DR PDB; 4GYS; X-ray; 2.20 A; A/B=1-592. DR PDBsum; 4GYR; -. DR PDBsum; 4GYS; -. DR AlphaFoldDB; Q0BRB0; -. DR SMR; Q0BRB0; -. DR STRING; 391165.GbCGDNIH1_1744; -. DR KEGG; gbe:GbCGDNIH1_1744; -. DR eggNOG; COG0154; Bacteria. DR HOGENOM; CLU_009600_0_1_5; -. DR OrthoDB; 7245165at2; -. DR BRENDA; 3.5.1.54; 14260. DR Proteomes; UP000001963; Chromosome. DR GO; GO:0004039; F:allophanate hydrolase activity; IEA:UniProtKB-EC. DR Gene3D; 1.20.58.1700; -; 1. DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1. DR Gene3D; 3.10.490.10; Gamma-glutamyl cyclotransferase-like; 1. DR InterPro; IPR014085; Allophanate_hydrolase. DR InterPro; IPR000120; Amidase. DR InterPro; IPR023631; Amidase_dom. DR InterPro; IPR036928; AS_sf. DR NCBIfam; TIGR02713; allophanate_hyd; 1. DR PANTHER; PTHR11895:SF169; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE; 1. DR PANTHER; PTHR11895; TRANSAMIDASE; 1. DR Pfam; PF01425; Amidase; 1. DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4GYR, ECO:0007829|PDB:4GYS}; KW Hydrolase {ECO:0000313|EMBL:ABI62642.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001963}. FT DOMAIN 23..430 FT /note="Amidase" FT /evidence="ECO:0000259|Pfam:PF01425" SQ SEQUENCE 592 AA; 63014 MW; 063BB2E111F91A59 CRC64; MTLSMTLEGI QAFLAQGGTI EQVVTEAYDR ITRYGDKAVW IALRPREEVL AEARALDASP ATGKPLYGVP FAVKDNIDVA GLPCSAACPA FTYEPDRDAT VVARLRAAGA IVLGKTNLDQ FATGLVGTRS PFGAPRCVFD QDYISGGSSS GSAVAVAAGL VAFSLGTDTA GSGRVPAAFN NLVGVKPTKG LLSTSGVVPA CRSLDCVTVF AASVAEGTLI RRIAEGYDAA DPYSRPSQKR RLPHVGLRVG VPRQDQREFY GNTAYAALYQ RALDEMISLD AELVEIDFAP FRDAAKLLYG GPWVAERLEA VGDHLSRAPD SFDPVVRSIV ETAKTLSAVD AFRGQYELAA LTQQANAQWA RMDILLLPTA PTIHKVEAVM ADPVRLNSQL GHYTNFVNLL DCAAIAVPAG FIETGLPFGV TLVGPAFSDD SMALIADRLH RRLEPGYGQD RASLPDPVLE ETNPEQIALA VVGAHLSGQP LHWQLTERNA TLVARTRTAP EYRLYALAET IPPKPGLVAD PDFTGDGIEI ELWSMDAEAF GTFTALVPAP LAIGTLRLAD GTSVKGFVCE PAGLVGAQDI TRFGGWRAYL AQ //