ID A8I4S4_AZOC5 Unreviewed; 571 AA.
AC A8I4S4;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
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 OrderedLocusNames=AZC_1766 {ECO:0000313|EMBL:BAF87764.1};
OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Azorhizobium.
OX NCBI_TaxID=438753 {ECO:0000313|EMBL:BAF87764.1, ECO:0000313|Proteomes:UP000000270};
RN [1] {ECO:0000313|EMBL:BAF87764.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=17720818; DOI=10.1128/AEM.01514-07;
RA Suzuki S., Aono T., Lee KB., Suzuki T., Liu CT., Miwa H., Wakao S., Iki T.,
RA Oyaizu H.;
RT "Rhizobial factors required for stem nodule maturation and maintenance in
RT Sesbania rostrata-Azorhizobium caulinodans ORS571 symbiosis.";
RL Appl. Environ. Microbiol. 73:6650-6659(2007).
RN [2] {ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT caulinodans ORS571.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:BAF87764.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=18522759; DOI=10.1186/1471-2164-9-271;
RA Lee KB., Backer P.D., Aono T., Liu CT., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T.T., Ussery D.W., D'Haeze W., Herder J.D., Gevers D.,
RA Vereecke D., Holsters M., Oyaizu H.;
RT "The genome of the versatile nitrogen fixer Azorhizobium caulinodans
RT ORS571.";
RL BMC Genomics 9:271-271(2008).
RN [4] {ECO:0000313|EMBL:BAF87764.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=19542345; DOI=10.1128/AEM.00398-09;
RA Tsukada S., Aono T., Akiba N., Lee KB., Liu CT., Toyazaki H., Oyaizu H.;
RT "Comparative genome-wide transcriptional profiling of Azorhizobium
RT caulinodans ORS571 grown under free-living and symbiotic conditions.";
RL Appl. Environ. Microbiol. 75:5037-5046(2009).
RN [5] {ECO:0000313|EMBL:BAF87764.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=20382809; DOI=10.1128/AEM.00238-10;
RA Akiba N., Aono T., Toyazaki H., Sato S., Oyaizu H.;
RT "phrR-like gene praR of Azorhizobium caulinodans ORS571 is essential for
RT symbiosis with Sesbania rostrata and is involved in expression of reb
RT genes.";
RL Appl. Environ. Microbiol. 76:3475-3485(2010).
RN [6] {ECO:0000313|EMBL:BAF87764.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=21571889; DOI=10.1128/AEM.02327-10;
RA Liu CT., Lee KB., Wang YS., Peng MH., Lee KT., Suzuki S., Suzuki T.,
RA Oyaizu H.;
RT "Involvement of the azorhizobial chromosome partition gene (parA) in the
RT onset of bacteroid differentiation during Sesbania rostrata stem nodule
RT development.";
RL Appl. Environ. Microbiol. 77:4371-4382(2011).
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; AP009384; BAF87764.1; -; Genomic_DNA.
DR RefSeq; WP_012170294.1; NC_009937.1.
DR AlphaFoldDB; A8I4S4; -.
DR STRING; 438753.AZC_1766; -.
DR MEROPS; M38.982; -.
DR KEGG; azc:AZC_1766; -.
DR eggNOG; COG0804; Bacteria.
DR HOGENOM; CLU_000980_0_0_5; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000000270; 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:UP000000270}.
FT DOMAIN 132..571
FT /note="Urease"
FT /evidence="ECO:0000259|PROSITE:PS51368"
FT ACT_SITE 323
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-52"
FT BINDING 137
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 139
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 220
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 220
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 222
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 249
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 275
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 363
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 220
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-50"
SQ SEQUENCE 571 AA; 60689 MW; E1165CE0AB925285 CRC64;
MTKARMSRSA YAHMFGPTVG DKVRLADTAL YIEIEKDFTV HGEEVKFGGG KVIRDGMGQS
QVANADGAVD TVITNAVILD HWGIVKADVG LKDGRIFKIG KAGNPDVQSG VDIIIGPGTE
VIAGEGKILT AGGFDSHIHF ICPQQIEEAL ASGVTTMLGG GTGPATGTFA TTCTPGPWHI
ARMIEAADAF PMNLAFAGKG NASQPKALEE MVRAGACALK LHEDWGTTPA AIDTCLSVAD
AFDIQVMIHT DTLNESGFVE DTIAAFKGRT IHAFHTEGAG GGHAPDIIKV AGLPNVLPSS
TNPTRPYTRN TIDEHLDMLM VCHHLSPSIP EDLAFAESRI RKETIAAEDI LHDIGALSMM
SSDSQAMGRV GEVVIRTWQT ADKMKRQRGA LPGESGGNDN LRARRYVAKY TINPAIAHGV
SKHIGSVEAG KLADLVLWSP AFFGVKPDLV LKGGSIAVAQ MGDPNASIPT PQPVHYRPMF
GAYGRARTHS SLTFVSKAAV EDGLAARLQT AKTLVAVENV RSGISKKDMV LNGATPHIEV
DPETYDVRAD GELLVCEPAD VLPMAQRYFL F
//
