ID A0A0B5E2K0_9RHOB Unreviewed; 465 AA.
AC A0A0B5E2K0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=S-adenosylhomocysteine deaminase, methylthioadenosine deaminase {ECO:0000313|EMBL:AJE46662.1};
GN ORFNames=P73_1947 {ECO:0000313|EMBL:AJE46662.1};
OS Celeribacter indicus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208324 {ECO:0000313|EMBL:AJE46662.1, ECO:0000313|Proteomes:UP000031521};
RN [1] {ECO:0000313|EMBL:AJE46662.1, ECO:0000313|Proteomes:UP000031521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P73 {ECO:0000313|EMBL:AJE46662.1};
RX PubMed=25256706; DOI=10.1099/ijs.0.069039-0;
RA Lai Q., Cao J., Yuan J., Li F., Shao Z.;
RT "Celeribacter indicus sp. nov., a polycyclic aromatic hydrocarbon-degrading
RT bacterium from deep-sea sediment and reclassification of Huaishuia
RT halophila as Celeribacter halophilus comb. nov.";
RL Int. J. Syst. Evol. Microbiol. 64:4160-4167(2014).
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000256|ARBA:ARBA00006745}.
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DR EMBL; CP004393; AJE46662.1; -; Genomic_DNA.
DR RefSeq; WP_043869437.1; NZ_FNNW01000043.1.
DR AlphaFoldDB; A0A0B5E2K0; -.
DR STRING; 1208324.P73_1947; -.
DR KEGG; cid:P73_1947; -.
DR HOGENOM; CLU_012358_2_1_5; -.
DR OrthoDB; 9796020at2; -.
DR Proteomes; UP000031521; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43794:SF11; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43794; AMINOHYDROLASE SSNA-RELATED; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000031521}.
FT DOMAIN 66..431
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 465 AA; 51367 MW; 3D921D997C2501E7 CRC64;
MNAPKTAPEC ADILIRRAHV VTLDPENRVI SQGAIAISGN RIAWIGKDSD AAKIQAKEVI
DANDQIAMPG LIDAHFHTGQ QLLRGKLQAI ARSRPLKLPV WKNYLIPWES CLDPEDVHLS
GLVAYTNMIQ VGTTCFAEAG GPHPDEMGRA ALEVGIRGFI SQSTVDQSEN IGATVPPNML
LTHDEALEKN TSLVDRWKDG DRVKAWMSLR QVIVCSPELI RDITVEAQSR DVKIHTHLCE
GSYEIDYTAE KFGMRPTEWL ESMGVLSHRL HCAHSVLLSD RELDLYEQHS LSACHCGFGN
YSIGHPRLIE MWRRGIDIGL GTDGPGGGGT IDLFQVAHVA RVGQQAIHSS TLHWKDPISS
EELLRVATHG GARALGIFDH VGSLEVGKKA DILLADTSRM DHRPMQDPLF IAASVLVGRD
MDTVLVDGRV VMRKREMVGI DVERINARLI ERMPIISERF EKLVG
//
