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Database: UniProt
Entry: D3NWP5_AZOS1
LinkDB: D3NWP5_AZOS1
Original site: D3NWP5_AZOS1 
ID   D3NWP5_AZOS1            Unreviewed;       569 AA.
AC   D3NWP5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=Urease subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953};
DE            EC=3.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01953};
DE   AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953};
GN   Name=ureC {ECO:0000256|HAMAP-Rule:MF_01953,
GN   ECO:0000313|EMBL:BAI72824.1};
GN   OrderedLocusNames=AZL_021860 {ECO:0000313|EMBL:BAI72824.1};
OS   Azospirillum sp. (strain B510).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI72824.1, ECO:0000313|Proteomes:UP000002040};
RN   [1] {ECO:0000313|EMBL:BAI72824.1, ECO:0000313|Proteomes:UP000002040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B510 {ECO:0000313|EMBL:BAI72824.1,
RC   ECO:0000313|Proteomes:UP000002040};
RX   PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA   Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA   Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA   Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA   Nakayama S., Yamada M., Tabata S., Sato S.;
RT   "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT   sp. B510.";
RL   DNA Res. 17:37-50(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01953,
CC         ECO:0000256|RuleBase:RU000510};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01953,
CC         ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1. {ECO:0000256|ARBA:ARBA00004897,
CC       ECO:0000256|HAMAP-Rule:MF_01953}.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha)
CC       subunits. Three heterotrimers associate to form the active enzyme.
CC       {ECO:0000256|HAMAP-Rule:MF_01953}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PROSITE-ProRule:PRU00700}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR611612-50}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|HAMAP-Rule:MF_01953}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Urease alpha subunit family. {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|RuleBase:RU004158}.
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DR   EMBL; AP010946; BAI72824.1; -; Genomic_DNA.
DR   RefSeq; WP_012974751.1; NC_013854.1.
DR   AlphaFoldDB; D3NWP5; -.
DR   STRING; 137722.AZL_021860; -.
DR   MEROPS; M38.982; -.
DR   KEGG; azl:AZL_021860; -.
DR   HOGENOM; CLU_000980_0_0_5; -.
DR   OrthoDB; 9802793at2; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000002040; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00375; Urease_alpha; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   HAMAP; MF_01953; Urease_alpha; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   InterPro; IPR017950; Urease_AS.
DR   InterPro; IPR005848; Urease_asu.
DR   InterPro; IPR017951; Urease_asu_c.
DR   InterPro; IPR029754; Urease_Ni-bd.
DR   NCBIfam; TIGR01792; urease_alph; 1.
DR   PANTHER; PTHR43440; UREASE; 1.
DR   PANTHER; PTHR43440:SF1; UREASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   PRINTS; PR01752; UREASE.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS01120; UREASE_1; 1.
DR   PROSITE; PS00145; UREASE_2; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW   ProRule:PRU00700};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01953};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01953};
KW   Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_01953};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002040}.
FT   DOMAIN          131..569
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        322
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-52"
FT   BINDING         136
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         138
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         219
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         219
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   BINDING         248
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         274
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         362
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-51"
FT   MOD_RES         219
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT                   ECO:0000256|PIRSR:PIRSR611612-50"
SQ   SEQUENCE   569 AA;  61049 MW;  EA445CAC5DC9556C CRC64;
     MAHRIDRAEY AALYGPTTGD RIRLADTDLI VEVERDHTVY GEEVKFGGGK VIRDGMGQSQ
     RSRHQGAVDT VITNALIIDH WGIVKADIGI TGGRIAAIGK AGNPDIQPGV DIIIGPGTEV
     IAGEGKIVTA GGIDAHIHFI CPQQVDEALN SGVTTMLGGG TGPAAGTSAT TCTPGPWHME
     RMLQAAEGLP INLGFFGKGN SSRPDALLEQ IAAGACGLKL HEDWGTTPDA IDTCLTVADQ
     LDVQVAIHTD TLNESGFVED TIAAFKGRTI HTFHTEGAGG GHAPDIIRVA SLANVLPSST
     NPTRPFTINT VDEHLDMLMV CHHLSPRIPE DVAFAESRIR RETIAAEDIL HDLGVFSMIS
     SDSQAMGRLG EVVIRTWQTA HKMKLQRGRL PQETGDNDNF RVKRYIAKYT INPALSHGIG
     HVVGSVEVGK LADLVLWSPA FFGVKPDMVI KCGTIAAALM GDPNASIPTP QPVHYRPMFG
     AFGRAMQASS VTFVSAKALE REVGRHLGLH RELIAVRGTR GVGKADMIHN DAMPHIEVDP
     ETYEVRADGQ LLTCEPAEIL PMAQRYFLF
//
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