ID F5SX33_9GAMM Unreviewed; 553 AA.
AC F5SX33;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Formylmethanofuran dehydrogenase subunit A {ECO:0000313|EMBL:EGL54926.1};
GN ORFNames=MAMP_01920 {ECO:0000313|EMBL:EGL54926.1};
OS Methylophaga aminisulfidivorans MP.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL54926.1, ECO:0000313|Proteomes:UP000003544};
RN [1] {ECO:0000313|EMBL:EGL54926.1, ECO:0000313|Proteomes:UP000003544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX PubMed=21685284; DOI=10.1128/JB.05403-11;
RA Han G.H., Kim W., Chun J., Kim S.W.;
RT "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL J. Bacteriol. 193:4265-4265(2011).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGL54926.1}.
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DR EMBL; AFIG01000001; EGL54926.1; -; Genomic_DNA.
DR RefSeq; WP_007144812.1; NZ_AFIG01000001.1.
DR AlphaFoldDB; F5SX33; -.
DR STRING; 1026882.MAMP_01920; -.
DR eggNOG; COG1229; Bacteria.
DR OrthoDB; 9807210at2; -.
DR Proteomes; UP000003544; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR012027; Formylmethanofuran_DH_asu.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR03121; one_C_dehyd_A; 1.
DR PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR PIRSF; PIRSF006453; FwdA; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000003544}.
FT DOMAIN 45..484
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 553 AA; 61901 MW; E306034DC59F86D4 CRC64;
MYSCIKNARA YDPVQNWHGE IRDIWFRDDR ICNAPAIEQQ QKATIYDVNG DIVMAGGIDI
HSHIAGGNVN TARLLLPEQH RNHLMRQAAT PFANARWSSF ETGYKYTEMG YSMVVEPAML
PVNAPQVHAE FADIPIIDTA ALAILGSDDL LVNLIRQGGS QSQINDYVAW MLHKTKALGL
KVINAGGSQA FKDGAETFNL DDVLTDYSIS SRQLLQTLQT AAVQTGLPHP VHVHCNNLGT
PGNIQTIVDT MEAAQGLPMH LAHVQFYGYG NEGKFGFSSA AAQLMAAFNR YPNITMDVGQ
VLFGQTVTLS GDVMAQFARR GDASPNKWHV WHAENEGSGG IVPYQYKQTS FVNGLQWAIG
LEIFLLSEDP WRLFFTTDHP NGAPFTRYPD LLHLLMSYDY RMACLENLHP EITEMTLLKD
LKKEFSLYEI AIMTRAAPAR LLGQKDRGTL QVGARADIAV YREREDKSAM FRHAEKVFKN
GQLVLDEGRV IQRTNGSTVT ASVGFNQEIE DTIQDYFDRF YTMKLSHYGI TDAFMEEQYR
DYLATKVSGQ YSA
//
