HUTG_BACSU
ID HUTG_BACSU Reviewed; 319 AA.
AC P42068;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Formimidoylglutamase {ECO:0000255|HAMAP-Rule:MF_00737};
DE EC=3.5.3.8 {ECO:0000255|HAMAP-Rule:MF_00737, ECO:0000269|PubMed:4990470};
DE AltName: Full=Formiminoglutamase {ECO:0000255|HAMAP-Rule:MF_00737};
DE AltName: Full=Formiminoglutamate hydrolase {ECO:0000255|HAMAP-Rule:MF_00737, ECO:0000303|PubMed:4990470};
DE AltName: Full=N-formimino-L-glutamate formiminohydrolase {ECO:0000303|PubMed:4990470};
GN Name=hutG {ECO:0000255|HAMAP-Rule:MF_00737}; OrderedLocusNames=BSU39380;
GN ORFNames=EE57C;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=7704263; DOI=10.1099/13500872-141-2-337;
RA Yoshida K., Sano H., Seki S., Oda M., Fujimura M., Fujita Y.;
RT "Cloning and sequencing of a 29 kb region of the Bacillus subtilis genome
RT containing the hut and wapA loci.";
RL Microbiology 141:337-343(1995).
RN [2]
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP PATHWAY.
RX PubMed=4990470; DOI=10.1016/s0021-9258(18)62959-x;
RA Kaminskas E., Kimhi Y., Magasanik B.;
RT "Urocanase and N-formimino-L-glutamate formiminohydrolase of Bacillus
RT subtilis, two enzymes of the histidine degradation pathway.";
RL J. Biol. Chem. 245:3536-3544(1970).
RN [4] {ECO:0007744|PDB:3M1R}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RA Tan K., Bigelow L., Buck K., Joachimiak A.;
RT "The crystal structure of formimidoylglutamase from Bacillus subtilis
RT subsp. subtilis str. 168.";
RL Submitted (MAR-2010) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the conversion of N-formimidoyl-L-glutamate to L-
CC glutamate and formamide. {ECO:0000255|HAMAP-Rule:MF_00737,
CC ECO:0000269|PubMed:4990470}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-formimidoyl-L-glutamate = formamide + L-glutamate;
CC Xref=Rhea:RHEA:22492, ChEBI:CHEBI:15377, ChEBI:CHEBI:16397,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58928; EC=3.5.3.8;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00737,
CC ECO:0000269|PubMed:4990470};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00737,
CC ECO:0000269|PubMed:4990470};
CC Note=Binds 2 manganese ions per subunit. Can also use other divalent
CC cation, with lower efficiency (PubMed:4990470).
CC {ECO:0000269|PubMed:4990470};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=4.4 mmol/min/mg enzyme (at pH 8.7) {ECO:0000269|PubMed:4990470};
CC Vmax=0.46 mmol/min/mg enzyme (at pH 7.4)
CC {ECO:0000269|PubMed:4990470};
CC pH dependence:
CC Optimum pH is 8.7. {ECO:0000269|PubMed:4990470};
CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; L-glutamate from N-formimidoyl-L-glutamate (hydrolase
CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00737,
CC ECO:0000269|PubMed:4990470}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|HAMAP-
CC Rule:MF_00737, ECO:0000305}.
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DR EMBL; D31856; BAA06641.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15974.1; -; Genomic_DNA.
DR PIR; B69643; B69643.
DR RefSeq; NP_391817.1; NC_000964.3.
DR RefSeq; WP_003243908.1; NZ_JNCM01000034.1.
DR PDB; 3M1R; X-ray; 2.20 A; A/B/C/D/E/F=1-319.
DR PDBsum; 3M1R; -.
DR AlphaFoldDB; P42068; -.
DR SMR; P42068; -.
DR STRING; 224308.BSU39380; -.
DR PaxDb; P42068; -.
DR PRIDE; P42068; -.
DR DNASU; 937546; -.
DR EnsemblBacteria; CAB15974; CAB15974; BSU_39380.
DR GeneID; 937546; -.
DR KEGG; bsu:BSU39380; -.
DR PATRIC; fig|224308.179.peg.4263; -.
DR eggNOG; COG0010; Bacteria.
DR InParanoid; P42068; -.
DR OMA; GTMFRQI; -.
DR PhylomeDB; P42068; -.
DR BioCyc; BSUB:BSU39380-MON; -.
DR BioCyc; MetaCyc:MON-11606; -.
DR UniPathway; UPA00379; UER00552.
DR EvolutionaryTrace; P42068; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008783; F:agmatinase activity; IBA:GO_Central.
DR GO; GO:0050415; F:formimidoylglutamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019556; P:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR GO; GO:0033389; P:putrescine biosynthetic process from arginine, using agmatinase; IBA:GO_Central.
DR HAMAP; MF_00737; Formimidoylglutam; 1.
DR InterPro; IPR005923; HutG.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR PANTHER; PTHR11358; PTHR11358; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01227; hutG; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Histidine metabolism; Hydrolase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..319
FT /note="Formimidoylglutamase"
FT /id="PRO_0000173749"
FT BINDING 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737,
FT ECO:0000305|Ref.4"
FT BINDING 150
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737,
FT ECO:0000305|Ref.4"
FT BINDING 150
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737,
FT ECO:0000305|Ref.4"
FT BINDING 152
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737,
FT ECO:0000305|Ref.4"
FT BINDING 154
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737,
FT ECO:0000305|Ref.4"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737,
FT ECO:0000305|Ref.4"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737,
FT ECO:0000305|Ref.4"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00737,
FT ECO:0000305|Ref.4"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:3M1R"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3M1R"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:3M1R"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3M1R"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:3M1R"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:3M1R"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:3M1R"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3M1R"
FT HELIX 97..114
FT /evidence="ECO:0007829|PDB:3M1R"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:3M1R"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:3M1R"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:3M1R"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:3M1R"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:3M1R"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:3M1R"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:3M1R"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:3M1R"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:3M1R"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:3M1R"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:3M1R"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:3M1R"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3M1R"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:3M1R"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:3M1R"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:3M1R"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:3M1R"
FT HELIX 297..315
FT /evidence="ECO:0007829|PDB:3M1R"
SQ SEQUENCE 319 AA; 35064 MW; BF158EE4301703A6 CRC64;
MDKYPFLREA GSSFKDRDVT KMSDLIATWD GQDIKGPALI GVPLSKSSIS HSGASFAPGT
IRQALKHSSA YSAELGEHVV SELLYDLGDI DIHVTDIVKS HHHIFQTMHA LLSDHPDWVP
LILGGDNSIS YSTIKAIAQT KGTTAVIQFD AHHDVRNTED GGPTNGTPFR RLLDEEIIEG
QHLIQLGIRE FSNSQAYEAY AKKHNVNIHT MDMIREKGLI PTIKEILPVV QDKTDFIFIS
VDMDVLDQSH APGCPAIGPG GLYTDELLEA VKYIAQQPNV AGIEIVEVDP TLDFRDMTSR
AAAHVLLHAL KGMKLSPFK
