ID   A0A0H5SDL9_HERHM        Unreviewed;      1262 AA.
AC   A0A0H5SDL9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CRZ33472.1};
GN   ORFNames=HHT355_0260 {ECO:0000313|EMBL:CRZ33472.1};
OS   Herbinix hemicellulosilytica.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Herbinix.
OX   NCBI_TaxID=1564487 {ECO:0000313|EMBL:CRZ33472.1, ECO:0000313|Proteomes:UP000236497};
RN   [1] {ECO:0000313|EMBL:CRZ33472.1, ECO:0000313|Proteomes:UP000236497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T3/55T {ECO:0000313|EMBL:CRZ33472.1,
RC   ECO:0000313|Proteomes:UP000236497};
RA   Wibberg Daniel;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CVTD020000008; CRZ33472.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H5SDL9; -.
DR   OrthoDB; 9804441at2; -.
DR   Proteomes; UP000236497; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd02203; PurL_repeat1; 1.
DR   CDD; cd02204; PurL_repeat2; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR010141; FGAM_synthase.
DR   InterPro; IPR041609; PurL_linker.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   NCBIfam; TIGR01857; FGAM-synthase; 1.
DR   PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   Pfam; PF18072; FGAR-AT_linker; 1.
DR   Pfam; PF13507; GATase_5; 1.
DR   SMART; SM01211; GATase_5; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236497}.
FT   DOMAIN          180..229
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          442..594
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   ACT_SITE        1103
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1233
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1235
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   1262 AA;  140332 MW;  949097E7962C9827 CRC64;
     MSSVRRIYVE KKEPYAVRAK ELEVELKNYL GIKGLKSVRV LNRYMIDNVS DDTYEKALNT
     VFMEPPVDIL FEEYLPINPG DRIFSVEYLP GQFDQRADSA EQCLKLLNEN EEPVIRSATT
     YVLSGDISDE EFQKIKAYCI NPVDSRETDE EKPDTLVAKF EEPEDVEILS GFINMNDEDL
     KKLYDSLNLA MTLADLRHIQ NYFRDTEKRD PYITEIRVLD TYWSDHCRHT TFLTELKDIK
     FEEGYYTEPI KAAFFCYTND REKFYKGRDD KYISLMDIAT LAMKKLKADG MLDDMEVSEE
     INACSIIVPV EIDGKTEEWL VFFKNETHNH PTEIEPFGGA ATCLGGAIRD PLSGRGYVYQ
     AMRVTGAADP TQPIEATMKG KLPQRKICTE AAKGYSSYGN QIGLATGLVD EVYHPGYVAK
     RLEIGAVMGA APRKYVKREK CEPGDIIILL GGRTGRDGIG GATGSSKIHT TKSIDTCGAE
     VQKGNPPTER KIQRLFRRPE VCLLIKKCND FGAGGVSVAI GELADGLHIY LDKVPKKYAG
     LDGTELAISE SQERMAVVVS PEDVGKFMSY AEEENLEAVA VAEVTDTGRL IMEWRGKKIV
     NISREFLNTN GAHQEADAFV TVPDKDNNYF KLGALPFIHE NISIKDKWLK ALADLNICSK
     KGLVEMFDSS IGASTVTMPY GGKYQRTPIQ TMVAKLPVLE GKCDSVSMMS YGFDPYLSSW
     SPFHGAVYAV ISSVAKIVAS GGDYSKIRFT FQEYFRRLGT DPKRWGEPLA ALLGAYDAQI
     KLGLAAIGGK DSMSGTFNDI DVPPTLVSFA VNMALAGDIV TTEFKYPGNK IVKFNIKKDA
     YDLPVYEQVK SLYGNLHKLM KDKKIVSAFA VSFGGIAEAV SKMAFGNKLG VNLYASLDEK
     ELFLPDYGSI IAEMKAKDVS LLPEYGFIAE DYDVIGEVTA DEALKYGDET ITLDEAYSAW
     SKTLEGVYPT RTERNVKTFE TKLFDAGKVY VAKNKVAKPR VFIPVFPGTN CEYDTMKAFE
     AAGAEVETVV FANMNADDIR ESVKNYEKAI RKAQIIMFAG GFSAGDEPDG SGKFAATIFR
     NEIIREAVND LLYNRDGLAL GICNGFQILI KLGLVPYGEI RPQDEDSPTL ITNKIGRHVS
     KTVYTKIVSN ASPWLMKAEL GGIYSIPSSH GEGRFVASKE WIEKLFKNGQ VATQYVDING
     NPTTDDEYNP NGSYYAIEGI ISPDGRVFGK MTHSERIGDH VAINISGNQN QHIFESGVEY
     FK
//